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+anno_start	anno_end	anno_text	entity_type	sentence	section
+21	55	JNK/p38-specific MAPK phosphatases	protein_type	A conserved motif in JNK/p38-specific MAPK phosphatases as a determinant for JNK1 recognition and inactivation	TITLE
+77	81	JNK1	protein	A conserved motif in JNK/p38-specific MAPK phosphatases as a determinant for JNK1 recognition and inactivation	TITLE
+0	33	Mitogen-activated protein kinases	protein_type	Mitogen-activated protein kinases (MAPKs), important in a large array of signalling pathways, are tightly controlled by a cascade of protein kinases and by MAPK phosphatases (MKPs).	ABSTRACT
+35	40	MAPKs	protein_type	Mitogen-activated protein kinases (MAPKs), important in a large array of signalling pathways, are tightly controlled by a cascade of protein kinases and by MAPK phosphatases (MKPs).	ABSTRACT
+133	148	protein kinases	protein_type	Mitogen-activated protein kinases (MAPKs), important in a large array of signalling pathways, are tightly controlled by a cascade of protein kinases and by MAPK phosphatases (MKPs).	ABSTRACT
+156	173	MAPK phosphatases	protein_type	Mitogen-activated protein kinases (MAPKs), important in a large array of signalling pathways, are tightly controlled by a cascade of protein kinases and by MAPK phosphatases (MKPs).	ABSTRACT
+175	179	MKPs	protein_type	Mitogen-activated protein kinases (MAPKs), important in a large array of signalling pathways, are tightly controlled by a cascade of protein kinases and by MAPK phosphatases (MKPs).	ABSTRACT
+0	4	MAPK	protein_type	MAPK signalling efficiency and specificity is modulated by protein–protein interactions between individual MAPKs and the docking motifs in cognate binding partners.	ABSTRACT
+107	112	MAPKs	protein_type	MAPK signalling efficiency and specificity is modulated by protein–protein interactions between individual MAPKs and the docking motifs in cognate binding partners.	ABSTRACT
+121	135	docking motifs	structure_element	MAPK signalling efficiency and specificity is modulated by protein–protein interactions between individual MAPKs and the docking motifs in cognate binding partners.	ABSTRACT
+56	63	D-motif	structure_element	Two types of docking interactions have been identified: D-motif-mediated interaction and FXF-docking interaction.	ABSTRACT
+89	112	FXF-docking interaction	site	Two types of docking interactions have been identified: D-motif-mediated interaction and FXF-docking interaction.	ABSTRACT
+19	36	crystal structure	evidence	Here we report the crystal structure of JNK1 bound to the catalytic domain of MKP7 at 2.4-Å resolution, providing high-resolution structural insight into the FXF-docking interaction.	ABSTRACT
+40	44	JNK1	protein	Here we report the crystal structure of JNK1 bound to the catalytic domain of MKP7 at 2.4-Å resolution, providing high-resolution structural insight into the FXF-docking interaction.	ABSTRACT
+45	53	bound to	protein_state	Here we report the crystal structure of JNK1 bound to the catalytic domain of MKP7 at 2.4-Å resolution, providing high-resolution structural insight into the FXF-docking interaction.	ABSTRACT
+58	74	catalytic domain	structure_element	Here we report the crystal structure of JNK1 bound to the catalytic domain of MKP7 at 2.4-Å resolution, providing high-resolution structural insight into the FXF-docking interaction.	ABSTRACT
+78	82	MKP7	protein	Here we report the crystal structure of JNK1 bound to the catalytic domain of MKP7 at 2.4-Å resolution, providing high-resolution structural insight into the FXF-docking interaction.	ABSTRACT
+158	181	FXF-docking interaction	site	Here we report the crystal structure of JNK1 bound to the catalytic domain of MKP7 at 2.4-Å resolution, providing high-resolution structural insight into the FXF-docking interaction.	ABSTRACT
+4	22	285FNFL288 segment	structure_element	The 285FNFL288 segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix αG. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.	ABSTRACT
+26	30	MKP7	protein	The 285FNFL288 segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix αG. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.	ABSTRACT
+51	67	hydrophobic site	site	The 285FNFL288 segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix αG. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.	ABSTRACT
+71	75	JNK1	protein	The 285FNFL288 segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix ��G. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.	ABSTRACT
+93	97	MAPK	protein_type	The 285FNFL288 segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix αG. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.	ABSTRACT
+112	117	helix	structure_element	The 285FNFL288 segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix αG. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.	ABSTRACT
+118	120	αG	structure_element	The 285FNFL288 segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix αG. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.	ABSTRACT
+122	141	Biochemical studies	experimental_method	The 285FNFL288 segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix αG. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.	ABSTRACT
+167	183	highly conserved	protein_state	The 285FNFL288 segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix αG. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.	ABSTRACT
+184	200	structural motif	structure_element	The 285FNFL288 segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix αG. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.	ABSTRACT
+234	244	MKP family	protein_type	The 285FNFL288 segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix αG. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.	ABSTRACT
+305	308	MKP	protein_type	The 285FNFL288 segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix αG. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.	ABSTRACT
+309	313	MAPK	protein_type	The 285FNFL288 segment in MKP7 directly binds to a hydrophobic site on JNK1 that is near the MAPK insertion and helix αG. Biochemical studies further reveal that this highly conserved structural motif is present in all members of the MKP family, and the interaction mode is universal and critical for the MKP-MAPK recognition and biological function.	ABSTRACT
+15	26	MAPK family	protein_type	 The important MAPK family of signalling proteins is controlled by MAPK phosphatases (MKPs).	ABSTRACT
+67	84	MAPK phosphatases	protein_type	 The important MAPK family of signalling proteins is controlled by MAPK phosphatases (MKPs).	ABSTRACT
+86	90	MKPs	protein_type	 The important MAPK family of signalling proteins is controlled by MAPK phosphatases (MKPs).	ABSTRACT
+29	38	structure	evidence	Here, the authors report the structure of MKP7 bound to JNK1 and characterise the conserved MKP-MAPK interaction.	ABSTRACT
+42	46	MKP7	protein	Here, the authors report the structure of MKP7 bound to JNK1 and characterise the conserved MKP-MAPK interaction.	ABSTRACT
+47	55	bound to	protein_state	Here, the authors report the structure of MKP7 bound to JNK1 and characterise the conserved MKP-MAPK interaction.	ABSTRACT
+56	60	JNK1	protein	Here, the authors report the structure of MKP7 bound to JNK1 and characterise the conserved MKP-MAPK interaction.	ABSTRACT
+82	91	conserved	protein_state	Here, the authors report the structure of MKP7 bound to JNK1 and characterise the conserved MKP-MAPK interaction.	ABSTRACT
+92	95	MKP	protein_type	Here, the authors report the structure of MKP7 bound to JNK1 and characterise the conserved MKP-MAPK interaction.	ABSTRACT
+96	100	MAPK	protein_type	Here, the authors report the structure of MKP7 bound to JNK1 and characterise the conserved MKP-MAPK interaction.	ABSTRACT
+4	37	mitogen-activated protein kinases	protein_type	The mitogen-activated protein kinases (MAPKs) are central components of the signal-transduction pathways, which mediate the cellular response to a variety of extracellular stimuli, ranging from growth factors to environmental stresses.	INTRO
+39	44	MAPKs	protein_type	The mitogen-activated protein kinases (MAPKs) are central components of the signal-transduction pathways, which mediate the cellular response to a variety of extracellular stimuli, ranging from growth factors to environmental stresses.	INTRO
+4	8	MAPK	protein_type	The MAPK signalling pathways are evolutionally highly conserved.	INTRO
+22	26	MAPK	protein_type	The basic assembly of MAPK pathways is a three-tier kinase module that establishes a sequential activation cascade: a MAPK kinase kinase activates a MAPK kinase, which in turn activates a MAPK.	INTRO
+52	58	kinase	protein_type	The basic assembly of MAPK pathways is a three-tier kinase module that establishes a sequential activation cascade: a MAPK kinase kinase activates a MAPK kinase, which in turn activates a MAPK.	INTRO
+118	136	MAPK kinase kinase	protein_type	The basic assembly of MAPK pathways is a three-tier kinase module that establishes a sequential activation cascade: a MAPK kinase kinase activates a MAPK kinase, which in turn activates a MAPK.	INTRO
+149	160	MAPK kinase	protein_type	The basic assembly of MAPK pathways is a three-tier kinase module that establishes a sequential activation cascade: a MAPK kinase kinase activates a MAPK kinase, which in turn activates a MAPK.	INTRO
+188	192	MAPK	protein_type	The basic assembly of MAPK pathways is a three-tier kinase module that establishes a sequential activation cascade: a MAPK kinase kinase activates a MAPK kinase, which in turn activates a MAPK.	INTRO
+29	33	MAPK	protein_type	The three best-characterized MAPK signalling pathways are mediated by the kinases extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK) and p38.	INTRO
+74	81	kinases	protein_type	The three best-characterized MAPK signalling pathways are mediated by the kinases extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK) and p38.	INTRO
+82	119	extracellular signal-regulated kinase	protein_type	The three best-characterized MAPK signalling pathways are mediated by the kinases extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK) and p38.	INTRO
+121	124	ERK	protein_type	The three best-characterized MAPK signalling pathways are mediated by the kinases extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK) and p38.	INTRO
+127	150	c-Jun N-terminal kinase	protein_type	The three best-characterized MAPK signalling pathways are mediated by the kinases extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK) and p38.	INTRO
+152	155	JNK	protein_type	The three best-characterized MAPK signalling pathways are mediated by the kinases extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK) and p38.	INTRO
+161	164	p38	protein_type	The three best-characterized MAPK signalling pathways are mediated by the kinases extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK) and p38.	INTRO
+4	7	ERK	protein_type	The ERK pathway is activated by various mitogens and phorbol esters, whereas the JNK and p38 pathways are stimulated mainly by environmental stress and inflammatory cytokines.	INTRO
+81	84	JNK	protein_type	The ERK pathway is activated by various mitogens and phorbol esters, whereas the JNK and p38 pathways are stimulated mainly by environmental stress and inflammatory cytokines.	INTRO
+89	92	p38	protein_type	The ERK pathway is activated by various mitogens and phorbol esters, whereas the JNK and p38 pathways are stimulated mainly by environmental stress and inflammatory cytokines.	INTRO
+165	174	cytokines	protein_type	The ERK pathway is activated by various mitogens and phorbol esters, whereas the JNK and p38 pathways are stimulated mainly by environmental stress and inflammatory cytokines.	INTRO
+4	9	MAPKs	protein_type	The MAPKs are activated by MAPK kinases that phosphorylate the MAPKs at conserved threonine and tyrosine residues within their activation loop.	INTRO
+27	39	MAPK kinases	protein_type	The MAPKs are activated by MAPK kinases that phosphorylate the MAPKs at conserved threonine and tyrosine residues within their activation loop.	INTRO
+63	68	MAPKs	protein_type	The MAPKs are activated by MAPK kinases that phosphorylate the MAPKs at conserved threonine and tyrosine residues within their activation loop.	INTRO
+72	81	conserved	protein_state	The MAPKs are activated by MAPK kinases that phosphorylate the MAPKs at conserved threonine and tyrosine residues within their activation loop.	INTRO
+82	91	threonine	residue_name	The MAPKs are activated by MAPK kinases that phosphorylate the MAPKs at conserved threonine and tyrosine residues within their activation loop.	INTRO
+96	104	tyrosine	residue_name	The MAPKs are activated by MAPK kinases that phosphorylate the MAPKs at conserved threonine and tyrosine residues within their activation loop.	INTRO
+127	142	activation loop	structure_element	The MAPKs are activated by MAPK kinases that phosphorylate the MAPKs at conserved threonine and tyrosine residues within their activation loop.	INTRO
+23	27	MAPK	protein_type	After activation, each MAPK phosphorylates a distinct set of protein substrates, which act as the critical effectors that enable cells to mount the appropriate responses to varied stimuli.	INTRO
+0	5	MAPKs	protein_type	MAPKs lie at the bottom of conserved three-component phosphorylation cascades and utilize docking interactions to link module components and bind substrates.	INTRO
+13	27	docking motifs	structure_element	Two types of docking motifs have been identified in MAPK substrates and cognate proteins: kinase-interacting motif (D-motif) and FXF-motif (also called DEF motif, docking site for ERK FXF).	INTRO
+52	56	MAPK	protein_type	Two types of docking motifs have been identified in MAPK substrates and cognate proteins: kinase-interacting motif (D-motif) and FXF-motif (also called DEF motif, docking site for ERK FXF).	INTRO
+90	114	kinase-interacting motif	structure_element	Two types of docking motifs have been identified in MAPK substrates and cognate proteins: kinase-interacting motif (D-motif) and FXF-motif (also called DEF motif, docking site for ERK FXF).	INTRO
+116	123	D-motif	structure_element	Two types of docking motifs have been identified in MAPK substrates and cognate proteins: kinase-interacting motif (D-motif) and FXF-motif (also called DEF motif, docking site for ERK FXF).	INTRO
+129	138	FXF-motif	structure_element	Two types of docking motifs have been identified in MAPK substrates and cognate proteins: kinase-interacting motif (D-motif) and FXF-motif (also called DEF motif, docking site for ERK FXF).	INTRO
+152	161	DEF motif	structure_element	Two types of docking motifs have been identified in MAPK substrates and cognate proteins: kinase-interacting motif (D-motif) and FXF-motif (also called DEF motif, docking site for ERK FXF).	INTRO
+163	175	docking site	site	Two types of docking motifs have been identified in MAPK substrates and cognate proteins: kinase-interacting motif (D-motif) and FXF-motif (also called DEF motif, docking site for ERK FXF).	INTRO
+180	183	ERK	protein_type	Two types of docking motifs have been identified in MAPK substrates and cognate proteins: kinase-interacting motif (D-motif) and FXF-motif (also called DEF motif, docking site for ERK FXF).	INTRO
+184	187	FXF	structure_element	Two types of docking motifs have been identified in MAPK substrates and cognate proteins: kinase-interacting motif (D-motif) and FXF-motif (also called DEF motif, docking site for ERK FXF).	INTRO
+56	67	MAP kinases	protein_type	The best-studied docking interactions are those between MAP kinases and ‘D-motifs', which consists of two or more basic residues followed by a short linker and a cluster of hydrophobic residues.	INTRO
+73	81	D-motifs	structure_element	The best-studied docking interactions are those between MAP kinases and ‘D-motifs', which consists of two or more basic residues followed by a short linker and a cluster of hydrophobic residues.	INTRO
+143	155	short linker	structure_element	The best-studied docking interactions are those between MAP kinases and ‘D-motifs', which consists of two or more basic residues followed by a short linker and a cluster of hydrophobic residues.	INTRO
+4	24	D-motif-docking site	site	The D-motif-docking site (D-site) in MAPKs is situated in a noncatalytic region opposite of the kinase catalytic pocket and is comprised of a highly acidic patch and a hydrophobic groove.	INTRO
+26	32	D-site	site	The D-motif-docking site (D-site) in MAPKs is situated in a noncatalytic region opposite of the kinase catalytic pocket and is comprised of a highly acidic patch and a hydrophobic groove.	INTRO
+37	42	MAPKs	protein_type	The D-motif-docking site (D-site) in MAPKs is situated in a noncatalytic region opposite of the kinase catalytic pocket and is comprised of a highly acidic patch and a hydrophobic groove.	INTRO
+60	79	noncatalytic region	site	The D-motif-docking site (D-site) in MAPKs is situated in a noncatalytic region opposite of the kinase catalytic pocket and is comprised of a highly acidic patch and a hydrophobic groove.	INTRO
+96	102	kinase	protein_type	The D-motif-docking site (D-site) in MAPKs is situated in a noncatalytic region opposite of the kinase catalytic pocket and is comprised of a highly acidic patch and a hydrophobic groove.	INTRO
+103	119	catalytic pocket	site	The D-motif-docking site (D-site) in MAPKs is situated in a noncatalytic region opposite of the kinase catalytic pocket and is comprised of a highly acidic patch and a hydrophobic groove.	INTRO
+142	161	highly acidic patch	site	The D-motif-docking site (D-site) in MAPKs is situated in a noncatalytic region opposite of the kinase catalytic pocket and is comprised of a highly acidic patch and a hydrophobic groove.	INTRO
+168	186	hydrophobic groove	site	The D-motif-docking site (D-site) in MAPKs is situated in a noncatalytic region opposite of the kinase catalytic pocket and is comprised of a highly acidic patch and a hydrophobic groove.	INTRO
+0	8	D-motifs	structure_element	D-motifs are found in many MAPK-interacting proteins, including substrates, activating kinases and inactivating phosphatases, as well as scaffolding proteins.	INTRO
+27	52	MAPK-interacting proteins	protein_type	D-motifs are found in many MAPK-interacting proteins, including substrates, activating kinases and inactivating phosphatases, as well as scaffolding proteins.	INTRO
+87	94	kinases	protein_type	D-motifs are found in many MAPK-interacting proteins, including substrates, activating kinases and inactivating phosphatases, as well as scaffolding proteins.	INTRO
+112	124	phosphatases	protein_type	D-motifs are found in many MAPK-interacting proteins, including substrates, activating kinases and inactivating phosphatases, as well as scaffolding proteins.	INTRO
+2	22	second docking motif	structure_element	A second docking motif for MAPKs consists of two Phe residues separated by one residue (FXF-motif).	INTRO
+27	32	MAPKs	protein_type	A second docking motif for MAPKs consists of two Phe residues separated by one residue (FXF-motif).	INTRO
+49	52	Phe	residue_name	A second docking motif for MAPKs consists of two Phe residues separated by one residue (FXF-motif).	INTRO
+88	97	FXF-motif	structure_element	A second docking motif for MAPKs consists of two Phe residues separated by one residue (FXF-motif).	INTRO
+40	44	MAPK	protein_type	This motif has been observed in several MAPK substrates.	INTRO
+4	26	FXF-motif-binding site	site	The FXF-motif-binding site of ERK2 has been mapped to a hydrophobic pocket formed between the P+1 site, αG helix and the MAPK insert.	INTRO
+30	34	ERK2	protein	The FXF-motif-binding site of ERK2 has been mapped to a hydrophobic pocket formed between the P+1 site, αG helix and the MAPK insert.	INTRO
+56	74	hydrophobic pocket	site	The FXF-motif-binding site of ERK2 has been mapped to a hydrophobic pocket formed between the P+1 site, αG helix and the MAPK insert.	INTRO
+94	102	P+1 site	site	The FXF-motif-binding site of ERK2 has been mapped to a hydrophobic pocket formed between the P+1 site, αG helix and the MAPK insert.	INTRO
+104	112	αG helix	structure_element	The FXF-motif-binding site of ERK2 has been mapped to a hydrophobic pocket formed between the P+1 site, αG helix and the MAPK insert.	INTRO
+121	132	MAPK insert	structure_element	The FXF-motif-binding site of ERK2 has been mapped to a hydrophobic pocket formed between the P+1 site, αG helix and the MAPK insert.	INTRO
+45	48	FXF	structure_element	However, the generality and mechanism of the FXF-mediated interaction is unclear.	INTRO
+29	33	MAPK	protein_type	The physiological outcome of MAPK signalling depends on both the magnitude and the duration of kinase activation.	INTRO
+18	22	MAPK	protein_type	Downregulation of MAPK activity can be achieved through direct dephosphorylation of the phospho-threonine and/or tyrosine residues by various serine/threonine phosphatases, tyrosine phosphatases and dual-specificity phosphatases (DUSPs) termed MKPs.	INTRO
+88	121	phospho-threonine and/or tyrosine	residue_name	Downregulation of MAPK activity can be achieved through direct dephosphorylation of the phospho-threonine and/or tyrosine residues by various serine/threonine phosphatases, tyrosine phosphatases and dual-specificity phosphatases (DUSPs) termed MKPs.	INTRO
+142	171	serine/threonine phosphatases	protein_type	Downregulation of MAPK activity can be achieved through direct dephosphorylation of the phospho-threonine and/or tyrosine residues by various serine/threonine phosphatases, tyrosine phosphatases and dual-specificity phosphatases (DUSPs) termed MKPs.	INTRO
+173	194	tyrosine phosphatases	protein_type	Downregulation of MAPK activity can be achieved through direct dephosphorylation of the phospho-threonine and/or tyrosine residues by various serine/threonine phosphatases, tyrosine phosphatases and dual-specificity phosphatases (DUSPs) termed MKPs.	INTRO
+199	228	dual-specificity phosphatases	protein_type	Downregulation of MAPK activity can be achieved through direct dephosphorylation of the phospho-threonine and/or tyrosine residues by various serine/threonine phosphatases, tyrosine phosphatases and dual-specificity phosphatases (DUSPs) termed MKPs.	INTRO
+230	235	DUSPs	protein_type	Downregulation of MAPK activity can be achieved through direct dephosphorylation of the phospho-threonine and/or tyrosine residues by various serine/threonine phosphatases, tyrosine phosphatases and dual-specificity phosphatases (DUSPs) termed MKPs.	INTRO
+244	248	MKPs	protein_type	Downregulation of MAPK activity can be achieved through direct dephosphorylation of the phospho-threonine and/or tyrosine residues by various serine/threonine phosphatases, tyrosine phosphatases and dual-specificity phosphatases (DUSPs) termed MKPs.	INTRO
+0	4	MKPs	protein_type	MKPs constitute a group of DUSPs that are characterized by their ability to dephosphorylate both phosphotyrosine and phosphoserine/phospho-threonine residues within a substrate.	INTRO
+27	32	DUSPs	protein_type	MKPs constitute a group of DUSPs that are characterized by their ability to dephosphorylate both phosphotyrosine and phosphoserine/phospho-threonine residues within a substrate.	INTRO
+97	112	phosphotyrosine	residue_name	MKPs constitute a group of DUSPs that are characterized by their ability to dephosphorylate both phosphotyrosine and phosphoserine/phospho-threonine residues within a substrate.	INTRO
+117	130	phosphoserine	residue_name	MKPs constitute a group of DUSPs that are characterized by their ability to dephosphorylate both phosphotyrosine and phosphoserine/phospho-threonine residues within a substrate.	INTRO
+131	148	phospho-threonine	residue_name	MKPs constitute a group of DUSPs that are characterized by their ability to dephosphorylate both phosphotyrosine and phosphoserine/phospho-threonine residues within a substrate.	INTRO
+27	31	MKPs	protein_type	Dysregulated expression of MKPs has been associated with pathogenesis of various diseases, and understanding their precise recognition mechanism presents an important challenge and opportunity for drug development.	INTRO
+21	38	crystal structure	evidence	Here, we present the crystal structure of JNK1 in complex with the catalytic domain of MKP7.	INTRO
+42	46	JNK1	protein	Here, we present the crystal structure of JNK1 in complex with the catalytic domain of MKP7.	INTRO
+47	62	in complex with	protein_state	Here, we present the crystal structure of JNK1 in complex with the catalytic domain of MKP7.	INTRO
+67	83	catalytic domain	structure_element	Here, we present the crystal structure of JNK1 in complex with the catalytic domain of MKP7.	INTRO
+87	91	MKP7	protein	Here, we present the crystal structure of JNK1 in complex with the catalytic domain of MKP7.	INTRO
+5	14	structure	evidence	This structure reveals the molecular mechanism underlying the docking interaction between MKP7 and JNK1.	INTRO
+90	94	MKP7	protein	This structure reveals the molecular mechanism underlying the docking interaction between MKP7 and JNK1.	INTRO
+99	103	JNK1	protein	This structure reveals the molecular mechanism underlying the docking interaction between MKP7 and JNK1.	INTRO
+7	16	JNK1–MKP7	complex_assembly	In the JNK1–MKP7 complex, a hydrophobic motif (285FNFL288) that initiates the helix α5 in the MKP7 catalytic domain directly binds to the FXF-motif-binding site on JNK1, providing the structural insight into the classic FXF-type docking interaction.	INTRO
+28	45	hydrophobic motif	structure_element	In the JNK1–MKP7 complex, a hydrophobic motif (285FNFL288) that initiates the helix α5 in the MKP7 catalytic domain directly binds to the FXF-motif-binding site on JNK1, providing the structural insight into the classic FXF-type docking interaction.	INTRO
+47	57	285FNFL288	structure_element	In the JNK1–MKP7 complex, a hydrophobic motif (285FNFL288) that initiates the helix α5 in the MKP7 catalytic domain directly binds to the FXF-motif-binding site on JNK1, providing the structural insight into the classic FXF-type docking interaction.	INTRO
+78	83	helix	structure_element	In the JNK1–MKP7 complex, a hydrophobic motif (285FNFL288) that initiates the helix α5 in the MKP7 catalytic domain directly binds to the FXF-motif-binding site on JNK1, providing the structural insight into the classic FXF-type docking interaction.	INTRO
+84	86	α5	structure_element	In the JNK1–MKP7 complex, a hydrophobic motif (285FNFL288) that initiates the helix α5 in the MKP7 catalytic domain directly binds to the FXF-motif-binding site on JNK1, providing the structural insight into the classic FXF-type docking interaction.	INTRO
+94	98	MKP7	protein	In the JNK1–MKP7 complex, a hydrophobic motif (285FNFL288) that initiates the helix α5 in the MKP7 catalytic domain directly binds to the FXF-motif-binding site on JNK1, providing the structural insight into the classic FXF-type docking interaction.	INTRO
+99	115	catalytic domain	structure_element	In the JNK1–MKP7 complex, a hydrophobic motif (285FNFL288) that initiates the helix α5 in the MKP7 catalytic domain directly binds to the FXF-motif-binding site on JNK1, providing the structural insight into the classic FXF-type docking interaction.	INTRO
+138	160	FXF-motif-binding site	site	In the JNK1–MKP7 complex, a hydrophobic motif (285FNFL288) that initiates the helix α5 in the MKP7 catalytic domain directly binds to the FXF-motif-binding site on JNK1, providing the structural insight into the classic FXF-type docking interaction.	INTRO
+164	168	JNK1	protein	In the JNK1–MKP7 complex, a hydrophobic motif (285FNFL288) that initiates the helix α5 in the MKP7 catalytic domain directly binds to the FXF-motif-binding site on JNK1, providing the structural insight into the classic FXF-type docking interaction.	INTRO
+220	248	FXF-type docking interaction	site	In the JNK1–MKP7 complex, a hydrophobic motif (285FNFL288) that initiates the helix α5 in the MKP7 catalytic domain directly binds to the FXF-motif-binding site on JNK1, providing the structural insight into the classic FXF-type docking interaction.	INTRO
+0	33	Biochemical and modelling studies	experimental_method	Biochemical and modelling studies further demonstrate that the molecular interactions mediate this key element for substrate recognition are highly conserved among all MKP-family members.	INTRO
+168	186	MKP-family members	protein_type	Biochemical and modelling studies further demonstrate that the molecular interactions mediate this key element for substrate recognition are highly conserved among all MKP-family members.	INTRO
+111	124	MAPK isoforms	protein_type	Thus, our study reveals a hitherto unrecognized interaction mode for encoding complex target specificity among MAPK isoforms.	INTRO
+15	19	JNK1	protein	Interaction of JNK1 with the MKP7 catalytic domain	RESULTS
+29	33	MKP7	protein	Interaction of JNK1 with the MKP7 catalytic domain	RESULTS
+34	50	catalytic domain	structure_element	Interaction of JNK1 with the MKP7 catalytic domain	RESULTS
+0	5	DUSPs	protein_type	DUSPs belong to the protein-tyrosine phosphatases (PTPase) superfamily, which is defined by the PTPase-signature motif CXXGXXR.	RESULTS
+20	49	protein-tyrosine phosphatases	protein_type	DUSPs belong to the protein-tyrosine phosphatases (PTPase) superfamily, which is defined by the PTPase-signature motif CXXGXXR.	RESULTS
+51	57	PTPase	protein_type	DUSPs belong to the protein-tyrosine phosphatases (PTPase) superfamily, which is defined by the PTPase-signature motif CXXGXXR.	RESULTS
+96	102	PTPase	protein_type	DUSPs belong to the protein-tyrosine phosphatases (PTPase) superfamily, which is defined by the PTPase-signature motif CXXGXXR.	RESULTS
+119	126	CXXGXXR	structure_element	DUSPs belong to the protein-tyrosine phosphatases (PTPase) superfamily, which is defined by the PTPase-signature motif CXXGXXR.	RESULTS
+0	4	MKPs	protein_type	MKPs represent a distinct subfamily within a larger group of DUSPs.	RESULTS
+61	66	DUSPs	protein_type	MKPs represent a distinct subfamily within a larger group of DUSPs.	RESULTS
+3	12	mammalian	taxonomy_domain	In mammalian cells, the MKP subfamily includes 10 distinct catalytically active MKPs.	RESULTS
+24	37	MKP subfamily	protein_type	In mammalian cells, the MKP subfamily includes 10 distinct catalytically active MKPs.	RESULTS
+59	79	catalytically active	protein_state	In mammalian cells, the MKP subfamily includes 10 distinct catalytically active MKPs.	RESULTS
+80	84	MKPs	protein_type	In mammalian cells, the MKP subfamily includes 10 distinct catalytically active MKPs.	RESULTS
+4	8	MKPs	protein_type	All MKPs contain a highly conserved C-terminal catalytic domain (CD) and an N-terminal kinase-binding domain (KBD).	RESULTS
+19	35	highly conserved	protein_state	All MKPs contain a highly conserved C-terminal catalytic domain (CD) and an N-terminal kinase-binding domain (KBD).	RESULTS
+47	63	catalytic domain	structure_element	All MKPs contain a highly conserved C-terminal catalytic domain (CD) and an N-terminal kinase-binding domain (KBD).	RESULTS
+65	67	CD	structure_element	All MKPs contain a highly conserved C-terminal catalytic domain (CD) and an N-terminal kinase-binding domain (KBD).	RESULTS
+87	108	kinase-binding domain	structure_element	All MKPs contain a highly conserved C-terminal catalytic domain (CD) and an N-terminal kinase-binding domain (KBD).	RESULTS
+110	113	KBD	structure_element	All MKPs contain a highly conserved C-terminal catalytic domain (CD) and an N-terminal kinase-binding domain (KBD).	RESULTS
+4	7	KBD	structure_element	The KBD is homologous to the rhodanese family and contains an intervening cluster of basic amino acids, which has been suggested to be important for interacting with the target MAPKs.	RESULTS
+29	45	rhodanese family	protein_type	The KBD is homologous to the rhodanese family and contains an intervening cluster of basic amino acids, which has been suggested to be important for interacting with the target MAPKs.	RESULTS
+177	182	MAPKs	protein_type	The KBD is homologous to the rhodanese family and contains an intervening cluster of basic amino acids, which has been suggested to be important for interacting with the target MAPKs.	RESULTS
+105	115	MKP family	protein_type	On the basis of sequence similarity, substrate specificity and predominant subcellular localization, the MKP family can be further divided into three groups (Fig. 1).	RESULTS
+0	34	Biochemical and structural studies	experimental_method	Biochemical and structural studies have revealed that the KBD of MKPs is critical for MKP3 docking to ERK2, and MKP5 binding to p38α, although their binding mechanisms are completely different.	RESULTS
+58	61	KBD	structure_element	Biochemical and structural studies have revealed that the KBD of MKPs is critical for MKP3 docking to ERK2, and MKP5 binding to p38α, although their binding mechanisms are completely different.	RESULTS
+65	69	MKPs	protein_type	Biochemical and structural studies have revealed that the KBD of MKPs is critical for MKP3 docking to ERK2, and MKP5 binding to p38α, although their binding mechanisms are completely different.	RESULTS
+86	90	MKP3	protein	Biochemical and structural studies have revealed that the KBD of MKPs is critical for MKP3 docking to ERK2, and MKP5 binding to p38α, although their binding mechanisms are completely different.	RESULTS
+102	106	ERK2	protein	Biochemical and structural studies have revealed that the KBD of MKPs is critical for MKP3 docking to ERK2, and MKP5 binding to p38α, although their binding mechanisms are completely different.	RESULTS
+112	116	MKP5	protein	Biochemical and structural studies have revealed that the KBD of MKPs is critical for MKP3 docking to ERK2, and MKP5 binding to p38α, although their binding mechanisms are completely different.	RESULTS
+128	132	p38α	protein	Biochemical and structural studies have revealed that the KBD of MKPs is critical for MKP3 docking to ERK2, and MKP5 binding to p38α, although their binding mechanisms are completely different.	RESULTS
+32	37	MAPKs	protein_type	However, it is unknown if other MAPKs can interact with the KBD of their cognate phosphatases in the same manner as observed for recognition of ERK2 and p38α by their MKPs, or whether they recognize distinct docking motifs of MKPs.	RESULTS
+60	63	KBD	structure_element	However, it is unknown if other MAPKs can interact with the KBD of their cognate phosphatases in the same manner as observed for recognition of ERK2 and p38α by their MKPs, or whether they recognize distinct docking motifs of MKPs.	RESULTS
+81	93	phosphatases	protein_type	However, it is unknown if other MAPKs can interact with the KBD of their cognate phosphatases in the same manner as observed for recognition of ERK2 and p38α by their MKPs, or whether they recognize distinct docking motifs of MKPs.	RESULTS
+144	148	ERK2	protein	However, it is unknown if other MAPKs can interact with the KBD of their cognate phosphatases in the same manner as observed for recognition of ERK2 and p38α by their MKPs, or whether they recognize distinct docking motifs of MKPs.	RESULTS
+153	157	p38α	protein	However, it is unknown if other MAPKs can interact with the KBD of their cognate phosphatases in the same manner as observed for recognition of ERK2 and p38α by their MKPs, or whether they recognize distinct docking motifs of MKPs.	RESULTS
+167	171	MKPs	protein_type	However, it is unknown if other MAPKs can interact with the KBD of their cognate phosphatases in the same manner as observed for recognition of ERK2 and p38α by their MKPs, or whether they recognize distinct docking motifs of MKPs.	RESULTS
+208	222	docking motifs	structure_element	However, it is unknown if other MAPKs can interact with the KBD of their cognate phosphatases in the same manner as observed for recognition of ERK2 and p38α by their MKPs, or whether they recognize distinct docking motifs of MKPs.	RESULTS
+226	230	MKPs	protein_type	However, it is unknown if other MAPKs can interact with the KBD of their cognate phosphatases in the same manner as observed for recognition of ERK2 and p38α by their MKPs, or whether they recognize distinct docking motifs of MKPs.	RESULTS
+0	4	MKP7	protein	MKP7, the biggest molecule in the MKP family, selectively inactivates JNK and p38 following stress activation.	RESULTS
+34	44	MKP family	protein_type	MKP7, the biggest molecule in the MKP family, selectively inactivates JNK and p38 following stress activation.	RESULTS
+70	73	JNK	protein_type	MKP7, the biggest molecule in the MKP family, selectively inactivates JNK and p38 following stress activation.	RESULTS
+78	81	p38	protein_type	MKP7, the biggest molecule in the MKP family, selectively inactivates JNK and p38 following stress activation.	RESULTS
+19	21	CD	structure_element	In addition to the CD and KBD, MKP7 has a long C-terminal region that contains both nuclear localization and export sequences by which MKP7 shuttles between the nucleus and the cytoplasm (Fig. 2a).	RESULTS
+26	29	KBD	structure_element	In addition to the CD and KBD, MKP7 has a long C-terminal region that contains both nuclear localization and export sequences by which MKP7 shuttles between the nucleus and the cytoplasm (Fig. 2a).	RESULTS
+31	35	MKP7	protein	In addition to the CD and KBD, MKP7 has a long C-terminal region that contains both nuclear localization and export sequences by which MKP7 shuttles between the nucleus and the cytoplasm (Fig. 2a).	RESULTS
+47	64	C-terminal region	structure_element	In addition to the CD and KBD, MKP7 has a long C-terminal region that contains both nuclear localization and export sequences by which MKP7 shuttles between the nucleus and the cytoplasm (Fig. 2a).	RESULTS
+135	139	MKP7	protein	In addition to the CD and KBD, MKP7 has a long C-terminal region that contains both nuclear localization and export sequences by which MKP7 shuttles between the nucleus and the cytoplasm (Fig. 2a).	RESULTS
+49	66	N-terminal domain	structure_element	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+74	78	MKP7	protein	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+89	93	JNK1	protein	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+94	111	dephosphorylation	ptm	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+135	142	kinetic	evidence	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+172	182	truncation	experimental_method	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+186	190	MKP7	protein	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+192	201	MKP7ΔC304	mutant	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+212	217	5–303	residue_range	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+223	227	MKP7	protein	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+228	230	CD	structure_element	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+241	248	156–301	residue_range	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+258	272	phosphorylated	protein_state	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+273	277	JNK1	protein	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+279	280	p	protein_state	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+280	284	JNK1	protein	To quantitatively assess the contribution of the N-terminal domain to the MKP7-catalysed JNK1 dephosphorylation, we first measured the kinetic parameters of the C-terminal truncation of MKP7 (MKP7ΔC304, residues 5–303) and MKP7-CD (residues 156–301) towards phosphorylated JNK1 (pJNK1).	RESULTS
+20	46	variation of initial rates	evidence	Figure 2b shows the variation of initial rates of the MKP7ΔC304 and MKP7-CD-catalysed reaction with the concentration of phospho-JNK1. Because the concentrations of MKP7 and pJNK1 were comparable in the reaction, the assumption that the free-substrate concentration is equal to the total substrate concentration is not valid.	RESULTS
+54	63	MKP7ΔC304	mutant	Figure 2b shows the variation of initial rates of the MKP7ΔC304 and MKP7-CD-catalysed reaction with the concentration of phospho-JNK1. Because the concentrations of MKP7 and pJNK1 were comparable in the reaction, the assumption that the free-substrate concentration is equal to the total substrate concentration is not valid.	RESULTS
+68	72	MKP7	protein	Figure 2b shows the variation of initial rates of the MKP7ΔC304 and MKP7-CD-catalysed reaction with the concentration of phospho-JNK1. Because the concentrations of MKP7 and pJNK1 were comparable in the reaction, the assumption that the free-substrate concentration is equal to the total substrate concentration is not valid.	RESULTS
+73	75	CD	structure_element	Figure 2b shows the variation of initial rates of the MKP7ΔC304 and MKP7-CD-catalysed reaction with the concentration of phospho-JNK1. Because the concentrations of MKP7 and pJNK1 were comparable in the reaction, the assumption that the free-substrate concentration is equal to the total substrate concentration is not valid.	RESULTS
+121	128	phospho	protein_state	Figure 2b shows the variation of initial rates of the MKP7ΔC304 and MKP7-CD-catalysed reaction with the concentration of phospho-JNK1. Because the concentrations of MKP7 and pJNK1 were comparable in the reaction, the assumption that the free-substrate concentration is equal to the total substrate concentration is not valid.	RESULTS
+129	133	JNK1	protein	Figure 2b shows the variation of initial rates of the MKP7ΔC304 and MKP7-CD-catalysed reaction with the concentration of phospho-JNK1. Because the concentrations of MKP7 and pJNK1 were comparable in the reaction, the assumption that the free-substrate concentration is equal to the total substrate concentration is not valid.	RESULTS
+165	169	MKP7	protein	Figure 2b shows the variation of initial rates of the MKP7ΔC304 and MKP7-CD-catalysed reaction with the concentration of phospho-JNK1. Because the concentrations of MKP7 and pJNK1 were comparable in the reaction, the assumption that the free-substrate concentration is equal to the total substrate concentration is not valid.	RESULTS
+174	175	p	protein_state	Figure 2b shows the variation of initial rates of the MKP7ΔC304 and MKP7-CD-catalysed reaction with the concentration of phospho-JNK1. Because the concentrations of MKP7 and pJNK1 were comparable in the reaction, the assumption that the free-substrate concentration is equal to the total substrate concentration is not valid.	RESULTS
+175	179	JNK1	protein	Figure 2b shows the variation of initial rates of the MKP7ΔC304 and MKP7-CD-catalysed reaction with the concentration of phospho-JNK1. Because the concentrations of MKP7 and pJNK1 were comparable in the reaction, the assumption that the free-substrate concentration is equal to the total substrate concentration is not valid.	RESULTS
+10	22	kinetic data	evidence	Thus, the kinetic data were analysed using the general initial velocity equation, taking substrate depletion into account:	RESULTS
+55	80	initial velocity equation	evidence	Thus, the kinetic data were analysed using the general initial velocity equation, taking substrate depletion into account:	RESULTS
+4	8	kcat	evidence	The kcat and Km of the MKP7-CD (0.028 s−1 and 0.26 μM) so determined were nearly identical to those of MKP7ΔC304 (0.029 s−1 and 0.27 μM), indicating that the MKP7-KBD has no effect on enzyme catalysis.	RESULTS
+13	15	Km	evidence	The kcat and Km of the MKP7-CD (0.028 s−1 and 0.26 μM) so determined were nearly identical to those of MKP7ΔC304 (0.029 s−1 and 0.27 μM), indicating that the MKP7-KBD has no effect on enzyme catalysis.	RESULTS
+23	27	MKP7	protein	The kcat and Km of the MKP7-CD (0.028 s−1 and 0.26 μM) so determined were nearly identical to those of MKP7ΔC304 (0.029 s−1 and 0.27 μM), indicating that the MKP7-KBD has no effect on enzyme catalysis.	RESULTS
+28	30	CD	structure_element	The kcat and Km of the MKP7-CD (0.028 s−1 and 0.26 μM) so determined were nearly identical to those of MKP7ΔC304 (0.029 s−1 and 0.27 μM), indicating that the MKP7-KBD has no effect on enzyme catalysis.	RESULTS
+103	112	MKP7ΔC304	mutant	The kcat and Km of the MKP7-CD (0.028 s−1 and 0.26 μM) so determined were nearly identical to those of MKP7ΔC304 (0.029 s−1 and 0.27 μM), indicating that the MKP7-KBD has no effect on enzyme catalysis.	RESULTS
+158	162	MKP7	protein	The kcat and Km of the MKP7-CD (0.028 s−1 and 0.26 μM) so determined were nearly identical to those of MKP7ΔC304 (0.029 s−1 and 0.27 μM), indicating that the MKP7-KBD has no effect on enzyme catalysis.	RESULTS
+163	166	KBD	structure_element	The kcat and Km of the MKP7-CD (0.028 s−1 and 0.26 μM) so determined were nearly identical to those of MKP7ΔC304 (0.029 s−1 and 0.27 μM), indicating that the MKP7-KBD has no effect on enzyme catalysis.	RESULTS
+36	40	JNK1	protein	We next examined the interaction of JNK1 with the CD and KBD of MKP7 by gel filtration analysis.	RESULTS
+50	52	CD	structure_element	We next examined the interaction of JNK1 with the CD and KBD of MKP7 by gel filtration analysis.	RESULTS
+57	60	KBD	structure_element	We next examined the interaction of JNK1 with the CD and KBD of MKP7 by gel filtration analysis.	RESULTS
+64	68	MKP7	protein	We next examined the interaction of JNK1 with the CD and KBD of MKP7 by gel filtration analysis.	RESULTS
+72	95	gel filtration analysis	experimental_method	We next examined the interaction of JNK1 with the CD and KBD of MKP7 by gel filtration analysis.	RESULTS
+28	30	CD	structure_element	When 3 molar equivalents of CD were mixed with 1 molar equivalent of JNK1, a significant amount of CD co-migrated with JNK1 to earlier fractions, and the excess amount of CD was eluted from the size exclusion column as a monomer, indicating stable complex formation (Fig. 2c).	RESULTS
+69	73	JNK1	protein	When 3 molar equivalents of CD were mixed with 1 molar equivalent of JNK1, a significant amount of CD co-migrated with JNK1 to earlier fractions, and the excess amount of CD was eluted from the size exclusion column as a monomer, indicating stable complex formation (Fig. 2c).	RESULTS
+99	101	CD	structure_element	When 3 molar equivalents of CD were mixed with 1 molar equivalent of JNK1, a significant amount of CD co-migrated with JNK1 to earlier fractions, and the excess amount of CD was eluted from the size exclusion column as a monomer, indicating stable complex formation (Fig. 2c).	RESULTS
+119	123	JNK1	protein	When 3 molar equivalents of CD were mixed with 1 molar equivalent of JNK1, a significant amount of CD co-migrated with JNK1 to earlier fractions, and the excess amount of CD was eluted from the size exclusion column as a monomer, indicating stable complex formation (Fig. 2c).	RESULTS
+171	173	CD	structure_element	When 3 molar equivalents of CD were mixed with 1 molar equivalent of JNK1, a significant amount of CD co-migrated with JNK1 to earlier fractions, and the excess amount of CD was eluted from the size exclusion column as a monomer, indicating stable complex formation (Fig. 2c).	RESULTS
+221	228	monomer	oligomeric_state	When 3 molar equivalents of CD were mixed with 1 molar equivalent of JNK1, a significant amount of CD co-migrated with JNK1 to earlier fractions, and the excess amount of CD was eluted from the size exclusion column as a monomer, indicating stable complex formation (Fig. 2c).	RESULTS
+16	24	KBD–JNK1	complex_assembly	In contrast, no KBD–JNK1 complex was detected when 3 molar equivalents of KBD were mixed with 1 molar equivalent of JNK1.	RESULTS
+74	77	KBD	structure_element	In contrast, no KBD–JNK1 complex was detected when 3 molar equivalents of KBD were mixed with 1 molar equivalent of JNK1.	RESULTS
+116	120	JNK1	protein	In contrast, no KBD–JNK1 complex was detected when 3 molar equivalents of KBD were mixed with 1 molar equivalent of JNK1.	RESULTS
+23	35	JNK1–MKP7-CD	complex_assembly	To further confirm the JNK1–MKP7-CD interaction, we performed a pull-down assay using the purified proteins.	RESULTS
+64	79	pull-down assay	experimental_method	To further confirm the JNK1–MKP7-CD interaction, we performed a pull-down assay using the purified proteins.	RESULTS
+25	27	CD	structure_element	As shown in Fig. 2d, the CD of MKP7 can be pulled down by JNK1, while the KBD failed to bind to the counterpart protein.	RESULTS
+31	35	MKP7	protein	As shown in Fig. 2d, the CD of MKP7 can be pulled down by JNK1, while the KBD failed to bind to the counterpart protein.	RESULTS
+58	62	JNK1	protein	As shown in Fig. 2d, the CD of MKP7 can be pulled down by JNK1, while the KBD failed to bind to the counterpart protein.	RESULTS
+74	77	KBD	structure_element	As shown in Fig. 2d, the CD of MKP7 can be pulled down by JNK1, while the KBD failed to bind to the counterpart protein.	RESULTS
+43	45	CD	structure_element	Taken together, our data indicate that the CD of MKP7, but not the KBD domain, is responsible for JNK substrate-binding and enzymatic specificity.	RESULTS
+49	53	MKP7	protein	Taken together, our data indicate that the CD of MKP7, but not the KBD domain, is responsible for JNK substrate-binding and enzymatic specificity.	RESULTS
+67	70	KBD	structure_element	Taken together, our data indicate that the CD of MKP7, but not the KBD domain, is responsible for JNK substrate-binding and enzymatic specificity.	RESULTS
+98	101	JNK	protein_type	Taken together, our data indicate that the CD of MKP7, but not the KBD domain, is responsible for JNK substrate-binding and enzymatic specificity.	RESULTS
+0	17	Crystal structure	evidence	Crystal structure of JNK1 in complex with the MKP7-CD	RESULTS
+21	25	JNK1	protein	Crystal structure of JNK1 in complex with the MKP7-CD	RESULTS
+26	41	in complex with	protein_state	Crystal structure of JNK1 in complex with the MKP7-CD	RESULTS
+46	50	MKP7	protein	Crystal structure of JNK1 in complex with the MKP7-CD	RESULTS
+51	53	CD	structure_element	Crystal structure of JNK1 in complex with the MKP7-CD	RESULTS
+37	41	JNK1	protein	To understand the molecular basis of JNK1 recognition by MKP7, we determined the crystal structure of unphosphorylated JNK1 in complex with the MKP7-CD (Fig. 3a, Supplementary Fig. 1a and Table 1).	RESULTS
+57	61	MKP7	protein	To understand the molecular basis of JNK1 recognition by MKP7, we determined the crystal structure of unphosphorylated JNK1 in complex with the MKP7-CD (Fig. 3a, Supplementary Fig. 1a and Table 1).	RESULTS
+81	98	crystal structure	evidence	To understand the molecular basis of JNK1 recognition by MKP7, we determined the crystal structure of unphosphorylated JNK1 in complex with the MKP7-CD (Fig. 3a, Supplementary Fig. 1a and Table 1).	RESULTS
+102	118	unphosphorylated	protein_state	To understand the molecular basis of JNK1 recognition by MKP7, we determined the crystal structure of unphosphorylated JNK1 in complex with the MKP7-CD (Fig. 3a, Supplementary Fig. 1a and Table 1).	RESULTS
+119	123	JNK1	protein	To understand the molecular basis of JNK1 recognition by MKP7, we determined the crystal structure of unphosphorylated JNK1 in complex with the MKP7-CD (Fig. 3a, Supplementary Fig. 1a and Table 1).	RESULTS
+124	139	in complex with	protein_state	To understand the molecular basis of JNK1 recognition by MKP7, we determined the crystal structure of unphosphorylated JNK1 in complex with the MKP7-CD (Fig. 3a, Supplementary Fig. 1a and Table 1).	RESULTS
+144	148	MKP7	protein	To understand the molecular basis of JNK1 recognition by MKP7, we determined the crystal structure of unphosphorylated JNK1 in complex with the MKP7-CD (Fig. 3a, Supplementary Fig. 1a and Table 1).	RESULTS
+149	151	CD	structure_element	To understand the molecular basis of JNK1 recognition by MKP7, we determined the crystal structure of unphosphorylated JNK1 in complex with the MKP7-CD (Fig. 3a, Supplementary Fig. 1a and Table 1).	RESULTS
+16	20	JNK1	protein	In the complex, JNK1 has its characteristic bilobal structure comprising an N-terminal lobe rich in β-sheet and a C-terminal lobe that is mostly α-helical.	RESULTS
+76	91	N-terminal lobe	structure_element	In the complex, JNK1 has its characteristic bilobal structure comprising an N-terminal lobe rich in β-sheet and a C-terminal lobe that is mostly α-helical.	RESULTS
+100	107	β-sheet	structure_element	In the complex, JNK1 has its characteristic bilobal structure comprising an N-terminal lobe rich in β-sheet and a C-terminal lobe that is mostly α-helical.	RESULTS
+114	129	C-terminal lobe	structure_element	In the complex, JNK1 has its characteristic bilobal structure comprising an N-terminal lobe rich in β-sheet and a C-terminal lobe that is mostly α-helical.	RESULTS
+145	154	α-helical	structure_element	In the complex, JNK1 has its characteristic bilobal structure comprising an N-terminal lobe rich in β-sheet and a C-terminal lobe that is mostly α-helical.	RESULTS
+23	27	MKP7	protein	The overall folding of MKP7-CD is typical of DUSPs, with a central twisted five-stranded β-sheet surrounded by six α-helices.	RESULTS
+28	30	CD	structure_element	The overall folding of MKP7-CD is typical of DUSPs, with a central twisted five-stranded β-sheet surrounded by six α-helices.	RESULTS
+45	50	DUSPs	protein_type	The overall folding of MKP7-CD is typical of DUSPs, with a central twisted five-stranded β-sheet surrounded by six α-helices.	RESULTS
+67	96	twisted five-stranded β-sheet	structure_element	The overall folding of MKP7-CD is typical of DUSPs, with a central twisted five-stranded β-sheet surrounded by six α-helices.	RESULTS
+115	124	α-helices	structure_element	The overall folding of MKP7-CD is typical of DUSPs, with a central twisted five-stranded β-sheet surrounded by six α-helices.	RESULTS
+16	23	β-sheet	structure_element	One side of the β-sheet is covered with two α-helices and the other is covered with four α-helices (Fig. 3b).	RESULTS
+44	53	α-helices	structure_element	One side of the β-sheet is covered with two α-helices and the other is covered with four α-helices (Fig. 3b).	RESULTS
+89	98	α-helices	structure_element	One side of the β-sheet is covered with two α-helices and the other is covered with four α-helices (Fig. 3b).	RESULTS
+4	20	catalytic domain	structure_element	The catalytic domain of MKP7 interacts with JNK1 through a contiguous surface area that is remote from the active site.	RESULTS
+24	28	MKP7	protein	The catalytic domain of MKP7 interacts with JNK1 through a contiguous surface area that is remote from the active site.	RESULTS
+44	48	JNK1	protein	The catalytic domain of MKP7 interacts with JNK1 through a contiguous surface area that is remote from the active site.	RESULTS
+107	118	active site	site	The catalytic domain of MKP7 interacts with JNK1 through a contiguous surface area that is remote from the active site.	RESULTS
+0	4	MKP7	protein	MKP7-CD is positioned onto the JNK1 molecule so that the active site of the phosphatase faces towards the activation segment.	RESULTS
+5	7	CD	structure_element	MKP7-CD is positioned onto the JNK1 molecule so that the active site of the phosphatase faces towards the activation segment.	RESULTS
+31	35	JNK1	protein	MKP7-CD is positioned onto the JNK1 molecule so that the active site of the phosphatase faces towards the activation segment.	RESULTS
+57	68	active site	site	MKP7-CD is positioned onto the JNK1 molecule so that the active site of the phosphatase faces towards the activation segment.	RESULTS
+76	87	phosphatase	protein_type	MKP7-CD is positioned onto the JNK1 molecule so that the active site of the phosphatase faces towards the activation segment.	RESULTS
+106	124	activation segment	structure_element	MKP7-CD is positioned onto the JNK1 molecule so that the active site of the phosphatase faces towards the activation segment.	RESULTS
+6	15	alignment	experimental_method	In an alignment of the structure of MKP7-CD with that of VHR, an atypical ‘MKP' consisting of only a catalytic domain, 119 of 147 MKP7-CD residues could be superimposed with a r.m.s.d. (root mean squared deviation) of 1.05 Å (Fig. 3c).	RESULTS
+23	32	structure	evidence	In an alignment of the structure of MKP7-CD with that of VHR, an atypical ‘MKP' consisting of only a catalytic domain, 119 of 147 MKP7-CD residues could be superimposed with a r.m.s.d. (root mean squared deviation) of 1.05 Å (Fig. 3c).	RESULTS
+36	40	MKP7	protein	In an alignment of the structure of MKP7-CD with that of VHR, an atypical ‘MKP' consisting of only a catalytic domain, 119 of 147 MKP7-CD residues could be superimposed with a r.m.s.d. (root mean squared deviation) of 1.05 Å (Fig. 3c).	RESULTS
+41	43	CD	structure_element	In an alignment of the structure of MKP7-CD with that of VHR, an atypical ‘MKP' consisting of only a catalytic domain, 119 of 147 MKP7-CD residues could be superimposed with a r.m.s.d. (root mean squared deviation) of 1.05 Å (Fig. 3c).	RESULTS
+57	60	VHR	protein	In an alignment of the structure of MKP7-CD with that of VHR, an atypical ‘MKP' consisting of only a catalytic domain, 119 of 147 MKP7-CD residues could be superimposed with a r.m.s.d. (root mean squared deviation) of 1.05 Å (Fig. 3c).	RESULTS
+75	78	MKP	protein_type	In an alignment of the structure of MKP7-CD with that of VHR, an atypical ‘MKP' consisting of only a catalytic domain, 119 of 147 MKP7-CD residues could be superimposed with a r.m.s.d. (root mean squared deviation) of 1.05 Å (Fig. 3c).	RESULTS
+101	117	catalytic domain	structure_element	In an alignment of the structure of MKP7-CD with that of VHR, an atypical ‘MKP' consisting of only a catalytic domain, 119 of 147 MKP7-CD residues could be superimposed with a r.m.s.d. (root mean squared deviation) of 1.05 Å (Fig. 3c).	RESULTS
+130	134	MKP7	protein	In an alignment of the structure of MKP7-CD with that of VHR, an atypical ‘MKP' consisting of only a catalytic domain, 119 of 147 MKP7-CD residues could be superimposed with a r.m.s.d. (root mean squared deviation) of 1.05 Å (Fig. 3c).	RESULTS
+135	137	CD	structure_element	In an alignment of the structure of MKP7-CD with that of VHR, an atypical ‘MKP' consisting of only a catalytic domain, 119 of 147 MKP7-CD residues could be superimposed with a r.m.s.d. (root mean squared deviation) of 1.05 Å (Fig. 3c).	RESULTS
+156	168	superimposed	experimental_method	In an alignment of the structure of MKP7-CD with that of VHR, an atypical ‘MKP' consisting of only a catalytic domain, 119 of 147 MKP7-CD residues could be superimposed with a r.m.s.d. (root mean squared deviation) of 1.05 Å (Fig. 3c).	RESULTS
+176	184	r.m.s.d.	evidence	In an alignment of the structure of MKP7-CD with that of VHR, an atypical ‘MKP' consisting of only a catalytic domain, 119 of 147 MKP7-CD residues could be superimposed with a r.m.s.d. (root mean squared deviation) of 1.05 Å (Fig. 3c).	RESULTS
+186	213	root mean squared deviation	evidence	In an alignment of the structure of MKP7-CD with that of VHR, an atypical ‘MKP' consisting of only a catalytic domain, 119 of 147 MKP7-CD residues could be superimposed with a r.m.s.d. (root mean squared deviation) of 1.05 Å (Fig. 3c).	RESULTS
+37	42	helix	structure_element	The most striking difference is that helix α0 and loop α0–β1 of VHR are absent in MKP7-CD.	RESULTS
+43	45	α0	structure_element	The most striking difference is that helix α0 and loop α0–β1 of VHR are absent in MKP7-CD.	RESULTS
+50	54	loop	structure_element	The most striking difference is that helix α0 and loop α0–β1 of VHR are absent in MKP7-CD.	RESULTS
+55	60	α0–β1	structure_element	The most striking difference is that helix α0 and loop α0–β1 of VHR are absent in MKP7-CD.	RESULTS
+64	67	VHR	protein	The most striking difference is that helix α0 and loop α0–β1 of VHR are absent in MKP7-CD.	RESULTS
+82	86	MKP7	protein	The most striking difference is that helix α0 and loop α0–β1 of VHR are absent in MKP7-CD.	RESULTS
+87	89	CD	structure_element	The most striking difference is that helix α0 and loop α0–β1 of VHR are absent in MKP7-CD.	RESULTS
+43	46	VHR	protein	Another region that cannot be aligned with VHR is found in loop β3–β4.	RESULTS
+59	63	loop	structure_element	Another region that cannot be aligned with VHR is found in loop β3–β4.	RESULTS
+64	69	β3–β4	structure_element	Another region that cannot be aligned with VHR is found in loop β3–β4.	RESULTS
+5	9	loop	structure_element	This loop is shortened by nine residues in MKP7-CD compared with that in VHR.	RESULTS
+43	47	MKP7	protein	This loop is shortened by nine residues in MKP7-CD compared with that in VHR.	RESULTS
+48	50	CD	structure_element	This loop is shortened by nine residues in MKP7-CD compared with that in VHR.	RESULTS
+73	76	VHR	protein	This loop is shortened by nine residues in MKP7-CD compared with that in VHR.	RESULTS
+6	11	helix	structure_element	Since helix α0 and the following loop α0–β1 are known for a substrate-recognition motif of VHR and other phosphatases, the absence of these moieties implicates a different substrate-binding mode of MKP7.	RESULTS
+12	14	α0	structure_element	Since helix α0 and the following loop α0–β1 are known for a substrate-recognition motif of VHR and other phosphatases, the absence of these moieties implicates a different substrate-binding mode of MKP7.	RESULTS
+33	37	loop	structure_element	Since helix α0 and the following loop α0–β1 are known for a substrate-recognition motif of VHR and other phosphatases, the absence of these moieties implicates a different substrate-binding mode of MKP7.	RESULTS
+38	43	α0–β1	structure_element	Since helix α0 and the following loop α0–β1 are known for a substrate-recognition motif of VHR and other phosphatases, the absence of these moieties implicates a different substrate-binding mode of MKP7.	RESULTS
+60	87	substrate-recognition motif	site	Since helix α0 and the following loop α0–β1 are known for a substrate-recognition motif of VHR and other phosphatases, the absence of these moieties implicates a different substrate-binding mode of MKP7.	RESULTS
+91	94	VHR	protein	Since helix α0 and the following loop α0–β1 are known for a substrate-recognition motif of VHR and other phosphatases, the absence of these moieties implicates a different substrate-binding mode of MKP7.	RESULTS
+105	117	phosphatases	protein_type	Since helix α0 and the following loop α0–β1 are known for a substrate-recognition motif of VHR and other phosphatases, the absence of these moieties implicates a different substrate-binding mode of MKP7.	RESULTS
+198	202	MKP7	protein	Since helix α0 and the following loop α0–β1 are known for a substrate-recognition motif of VHR and other phosphatases, the absence of these moieties implicates a different substrate-binding mode of MKP7.	RESULTS
+4	15	active site	site	The active site of MKP7 consists of the phosphate-binding loop (P-loop, Cys244-Leu245-Ala246-Gly247-Ile248-Ser249-Arg250), and Asp213 in the general acid loop (Fig. 3b and Supplementary Fig. 1b).	RESULTS
+19	23	MKP7	protein	The active site of MKP7 consists of the phosphate-binding loop (P-loop, Cys244-Leu245-Ala246-Gly247-Ile248-Ser249-Arg250), and Asp213 in the general acid loop (Fig. 3b and Supplementary Fig. 1b).	RESULTS
+40	62	phosphate-binding loop	structure_element	The active site of MKP7 consists of the phosphate-binding loop (P-loop, Cys244-Leu245-Ala246-Gly247-Ile248-Ser249-Arg250), and Asp213 in the general acid loop (Fig. 3b and Supplementary Fig. 1b).	RESULTS
+64	70	P-loop	structure_element	The active site of MKP7 consists of the phosphate-binding loop (P-loop, Cys244-Leu245-Ala246-Gly247-Ile248-Ser249-Arg250), and Asp213 in the general acid loop (Fig. 3b and Supplementary Fig. 1b).	RESULTS
+72	78	Cys244	residue_name_number	The active site of MKP7 consists of the phosphate-binding loop (P-loop, Cys244-Leu245-Ala246-Gly247-Ile248-Ser249-Arg250), and Asp213 in the general acid loop (Fig. 3b and Supplementary Fig. 1b).	RESULTS
+79	85	Leu245	residue_name_number	The active site of MKP7 consists of the phosphate-binding loop (P-loop, Cys244-Leu245-Ala246-Gly247-Ile248-Ser249-Arg250), and Asp213 in the general acid loop (Fig. 3b and Supplementary Fig. 1b).	RESULTS
+86	92	Ala246	residue_name_number	The active site of MKP7 consists of the phosphate-binding loop (P-loop, Cys244-Leu245-Ala246-Gly247-Ile248-Ser249-Arg250), and Asp213 in the general acid loop (Fig. 3b and Supplementary Fig. 1b).	RESULTS
+93	99	Gly247	residue_name_number	The active site of MKP7 consists of the phosphate-binding loop (P-loop, Cys244-Leu245-Ala246-Gly247-Ile248-Ser249-Arg250), and Asp213 in the general acid loop (Fig. 3b and Supplementary Fig. 1b).	RESULTS
+100	106	Ile248	residue_name_number	The active site of MKP7 consists of the phosphate-binding loop (P-loop, Cys244-Leu245-Ala246-Gly247-Ile248-Ser249-Arg250), and Asp213 in the general acid loop (Fig. 3b and Supplementary Fig. 1b).	RESULTS
+107	113	Ser249	residue_name_number	The active site of MKP7 consists of the phosphate-binding loop (P-loop, Cys244-Leu245-Ala246-Gly247-Ile248-Ser249-Arg250), and Asp213 in the general acid loop (Fig. 3b and Supplementary Fig. 1b).	RESULTS
+114	120	Arg250	residue_name_number	The active site of MKP7 consists of the phosphate-binding loop (P-loop, Cys244-Leu245-Ala246-Gly247-Ile248-Ser249-Arg250), and Asp213 in the general acid loop (Fig. 3b and Supplementary Fig. 1b).	RESULTS
+127	133	Asp213	residue_name_number	The active site of MKP7 consists of the phosphate-binding loop (P-loop, Cys244-Leu245-Ala246-Gly247-Ile248-Ser249-Arg250), and Asp213 in the general acid loop (Fig. 3b and Supplementary Fig. 1b).	RESULTS
+141	158	general acid loop	structure_element	The active site of MKP7 consists of the phosphate-binding loop (P-loop, Cys244-Leu245-Ala246-Gly247-Ile248-Ser249-Arg250), and Asp213 in the general acid loop (Fig. 3b and Supplementary Fig. 1b).	RESULTS
+4	8	MKP7	protein	The MKP7-CD structure near the active site exhibits a typical active conformation as found in VHR and other PTPs.	RESULTS
+9	11	CD	structure_element	The MKP7-CD structure near the active site exhibits a typical active conformation as found in VHR and other PTPs.	RESULTS
+12	21	structure	evidence	The MKP7-CD structure near the active site exhibits a typical active conformation as found in VHR and other PTPs.	RESULTS
+31	42	active site	site	The MKP7-CD structure near the active site exhibits a typical active conformation as found in VHR and other PTPs.	RESULTS
+62	81	active conformation	protein_state	The MKP7-CD structure near the active site exhibits a typical active conformation as found in VHR and other PTPs.	RESULTS
+94	97	VHR	protein	The MKP7-CD structure near the active site exhibits a typical active conformation as found in VHR and other PTPs.	RESULTS
+108	112	PTPs	protein_type	The MKP7-CD structure near the active site exhibits a typical active conformation as found in VHR and other PTPs.	RESULTS
+4	21	catalytic residue	site	The catalytic residue, Cys244, is located just after strand β5 and optimally positioned for nucleophilic attack.	RESULTS
+23	29	Cys244	residue_name_number	The catalytic residue, Cys244, is located just after strand β5 and optimally positioned for nucleophilic attack.	RESULTS
+53	59	strand	structure_element	The catalytic residue, Cys244, is located just after strand β5 and optimally positioned for nucleophilic attack.	RESULTS
+60	62	β5	structure_element	The catalytic residue, Cys244, is located just after strand β5 and optimally positioned for nucleophilic attack.	RESULTS
+0	6	Asp213	residue_name_number	Asp213 in MKP7 also adopts a position similar to that of Asp92 in VHR (Supplementary Fig. 1c), indicating that Asp213 is likely to function as the general acid in MKP7.	RESULTS
+10	14	MKP7	protein	Asp213 in MKP7 also adopts a position similar to that of Asp92 in VHR (Supplementary Fig. 1c), indicating that Asp213 is likely to function as the general acid in MKP7.	RESULTS
+57	62	Asp92	residue_name_number	Asp213 in MKP7 also adopts a position similar to that of Asp92 in VHR (Supplementary Fig. 1c), indicating that Asp213 is likely to function as the general acid in MKP7.	RESULTS
+66	69	VHR	protein	Asp213 in MKP7 also adopts a position similar to that of Asp92 in VHR (Supplementary Fig. 1c), indicating that Asp213 is likely to function as the general acid in MKP7.	RESULTS
+111	117	Asp213	residue_name_number	Asp213 in MKP7 also adopts a position similar to that of Asp92 in VHR (Supplementary Fig. 1c), indicating that Asp213 is likely to function as the general acid in MKP7.	RESULTS
+163	167	MKP7	protein	Asp213 in MKP7 also adopts a position similar to that of Asp92 in VHR (Supplementary Fig. 1c), indicating that Asp213 is likely to function as the general acid in MKP7.	RESULTS
+34	42	chloride	chemical	We also observed the binding of a chloride ion in the active site of MKP7-CD.	RESULTS
+54	65	active site	site	We also observed the binding of a chloride ion in the active site of MKP7-CD.	RESULTS
+69	73	MKP7	protein	We also observed the binding of a chloride ion in the active site of MKP7-CD.	RESULTS
+74	76	CD	structure_element	We also observed the binding of a chloride ion in the active site of MKP7-CD.	RESULTS
+30	36	Cys244	residue_name_number	It is located 3.36 Å from the Cys244 side chain and makes electrostatic interactions with the dipole moment of helix α3 and with several main-chain amide groups.	RESULTS
+58	84	electrostatic interactions	bond_interaction	It is located 3.36 Å from the Cys244 side chain and makes electrostatic interactions with the dipole moment of helix α3 and with several main-chain amide groups.	RESULTS
+111	116	helix	structure_element	It is located 3.36 Å from the Cys244 side chain and makes electrostatic interactions with the dipole moment of helix α3 and with several main-chain amide groups.	RESULTS
+117	119	α3	structure_element	It is located 3.36 Å from the Cys244 side chain and makes electrostatic interactions with the dipole moment of helix α3 and with several main-chain amide groups.	RESULTS
+18	36	strictly conserved	protein_state	The side chain of strictly conserved Arg250 is oriented towards the negatively charged chloride, similar to the canonical phosphate-coordinating conformation.	RESULTS
+37	43	Arg250	residue_name_number	The side chain of strictly conserved Arg250 is oriented towards the negatively charged chloride, similar to the canonical phosphate-coordinating conformation.	RESULTS
+87	95	chloride	chemical	The side chain of strictly conserved Arg250 is oriented towards the negatively charged chloride, similar to the canonical phosphate-coordinating conformation.	RESULTS
+122	157	phosphate-coordinating conformation	structure_element	The side chain of strictly conserved Arg250 is oriented towards the negatively charged chloride, similar to the canonical phosphate-coordinating conformation.	RESULTS
+10	18	chloride	chemical	Thus this chloride ion is a mimic for the phosphate group of the substrate, as revealed by a comparison with the structure of PTP1B in complex with phosphotyrosine (Supplementary Fig. 1d).	RESULTS
+42	51	phosphate	chemical	Thus this chloride ion is a mimic for the phosphate group of the substrate, as revealed by a comparison with the structure of PTP1B in complex with phosphotyrosine (Supplementary Fig. 1d).	RESULTS
+113	122	structure	evidence	Thus this chloride ion is a mimic for the phosphate group of the substrate, as revealed by a comparison with the structure of PTP1B in complex with phosphotyrosine (Supplementary Fig. 1d).	RESULTS
+126	131	PTP1B	protein	Thus this chloride ion is a mimic for the phosphate group of the substrate, as revealed by a comparison with the structure of PTP1B in complex with phosphotyrosine (Supplementary Fig. 1d).	RESULTS
+132	147	in complex with	protein_state	Thus this chloride ion is a mimic for the phosphate group of the substrate, as revealed by a comparison with the structure of PTP1B in complex with phosphotyrosine (Supplementary Fig. 1d).	RESULTS
+148	163	phosphotyrosine	residue_name	Thus this chloride ion is a mimic for the phosphate group of the substrate, as revealed by a comparison with the structure of PTP1B in complex with phosphotyrosine (Supplementary Fig. 1d).	RESULTS
+49	53	MKP7	protein	Although the catalytically important residues in MKP7-CD are well aligned with those in VHR, the residues in the P-loop of MKP7 are smaller and have a more hydrophobic character than those of VHR (Cys124-Arg125-Glu126-Gly127-Tyr128-Gly129-Arg130; Fig. 3b,c).	RESULTS
+54	56	CD	structure_element	Although the catalytically important residues in MKP7-CD are well aligned with those in VHR, the residues in the P-loop of MKP7 are smaller and have a more hydrophobic character than those of VHR (Cys124-Arg125-Glu126-Gly127-Tyr128-Gly129-Arg130; Fig. 3b,c).	RESULTS
+88	91	VHR	protein	Although the catalytically important residues in MKP7-CD are well aligned with those in VHR, the residues in the P-loop of MKP7 are smaller and have a more hydrophobic character than those of VHR (Cys124-Arg125-Glu126-Gly127-Tyr128-Gly129-Arg130; Fig. 3b,c).	RESULTS
+113	119	P-loop	structure_element	Although the catalytically important residues in MKP7-CD are well aligned with those in VHR, the residues in the P-loop of MKP7 are smaller and have a more hydrophobic character than those of VHR (Cys124-Arg125-Glu126-Gly127-Tyr128-Gly129-Arg130; Fig. 3b,c).	RESULTS
+123	127	MKP7	protein	Although the catalytically important residues in MKP7-CD are well aligned with those in VHR, the residues in the P-loop of MKP7 are smaller and have a more hydrophobic character than those of VHR (Cys124-Arg125-Glu126-Gly127-Tyr128-Gly129-Arg130; Fig. 3b,c).	RESULTS
+192	195	VHR	protein	Although the catalytically important residues in MKP7-CD are well aligned with those in VHR, the residues in the P-loop of MKP7 are smaller and have a more hydrophobic character than those of VHR (Cys124-Arg125-Glu126-Gly127-Tyr128-Gly129-Arg130; Fig. 3b,c).	RESULTS
+197	203	Cys124	residue_name_number	Although the catalytically important residues in MKP7-CD are well aligned with those in VHR, the residues in the P-loop of MKP7 are smaller and have a more hydrophobic character than those of VHR (Cys124-Arg125-Glu126-Gly127-Tyr128-Gly129-Arg130; Fig. 3b,c).	RESULTS
+204	210	Arg125	residue_name_number	Although the catalytically important residues in MKP7-CD are well aligned with those in VHR, the residues in the P-loop of MKP7 are smaller and have a more hydrophobic character than those of VHR (Cys124-Arg125-Glu126-Gly127-Tyr128-Gly129-Arg130; Fig. 3b,c).	RESULTS
+211	217	Glu126	residue_name_number	Although the catalytically important residues in MKP7-CD are well aligned with those in VHR, the residues in the P-loop of MKP7 are smaller and have a more hydrophobic character than those of VHR (Cys124-Arg125-Glu126-Gly127-Tyr128-Gly129-Arg130; Fig. 3b,c).	RESULTS
+218	224	Gly127	residue_name_number	Although the catalytically important residues in MKP7-CD are well aligned with those in VHR, the residues in the P-loop of MKP7 are smaller and have a more hydrophobic character than those of VHR (Cys124-Arg125-Glu126-Gly127-Tyr128-Gly129-Arg130; Fig. 3b,c).	RESULTS
+225	231	Tyr128	residue_name_number	Although the catalytically important residues in MKP7-CD are well aligned with those in VHR, the residues in the P-loop of MKP7 are smaller and have a more hydrophobic character than those of VHR (Cys124-Arg125-Glu126-Gly127-Tyr128-Gly129-Arg130; Fig. 3b,c).	RESULTS
+232	238	Gly129	residue_name_number	Although the catalytically important residues in MKP7-CD are well aligned with those in VHR, the residues in the P-loop of MKP7 are smaller and have a more hydrophobic character than those of VHR (Cys124-Arg125-Glu126-Gly127-Tyr128-Gly129-Arg130; Fig. 3b,c).	RESULTS
+239	245	Arg130	residue_name_number	Although the catalytically important residues in MKP7-CD are well aligned with those in VHR, the residues in the P-loop of MKP7 are smaller and have a more hydrophobic character than those of VHR (Cys124-Arg125-Glu126-Gly127-Tyr128-Gly129-Arg130; Fig. 3b,c).	RESULTS
+162	174	phosphatases	protein_type	The difference in the polarity/hydrophobicity of the surface may also point to the origin of the differences in the substrate-recognition mechanism for these two phosphatases (Supplementary Fig. 1e,f).	RESULTS
+16	20	MKP7	protein	In the complex, MKP7-CD and JNK1 form extensive protein–protein interactions involving the C-terminal helices of MKP7-CD and C-lobe of JNK1 (Fig. 3d,e).	RESULTS
+21	23	CD	structure_element	In the complex, MKP7-CD and JNK1 form extensive protein–protein interactions involving the C-terminal helices of MKP7-CD and C-lobe of JNK1 (Fig. 3d,e).	RESULTS
+28	32	JNK1	protein	In the complex, MKP7-CD and JNK1 form extensive protein–protein interactions involving the C-terminal helices of MKP7-CD and C-lobe of JNK1 (Fig. 3d,e).	RESULTS
+91	109	C-terminal helices	structure_element	In the complex, MKP7-CD and JNK1 form extensive protein–protein interactions involving the C-terminal helices of MKP7-CD and C-lobe of JNK1 (Fig. 3d,e).	RESULTS
+113	117	MKP7	protein	In the complex, MKP7-CD and JNK1 form extensive protein–protein interactions involving the C-terminal helices of MKP7-CD and C-lobe of JNK1 (Fig. 3d,e).	RESULTS
+118	120	CD	structure_element	In the complex, MKP7-CD and JNK1 form extensive protein–protein interactions involving the C-terminal helices of MKP7-CD and C-lobe of JNK1 (Fig. 3d,e).	RESULTS
+125	131	C-lobe	structure_element	In the complex, MKP7-CD and JNK1 form extensive protein–protein interactions involving the C-terminal helices of MKP7-CD and C-lobe of JNK1 (Fig. 3d,e).	RESULTS
+135	139	JNK1	protein	In the complex, MKP7-CD and JNK1 form extensive protein–protein interactions involving the C-terminal helices of MKP7-CD and C-lobe of JNK1 (Fig. 3d,e).	RESULTS
+76	93	C-terminal domain	structure_element	As a result, the buried solvent-accessible surface area is ∼1,315 Å. In the C-terminal domain, JNK1 has an insertion after the helix αG. This insertion consists of two helices (α1L14 and α2L14) that are common to all members of the MAPK family.	RESULTS
+95	99	JNK1	protein	As a result, the buried solvent-accessible surface area is ∼1,315 Å. In the C-terminal domain, JNK1 has an insertion after the helix αG. This insertion consists of two helices (α1L14 and α2L14) that are common to all members of the MAPK family.	RESULTS
+127	132	helix	structure_element	As a result, the buried solvent-accessible surface area is ∼1,315 Å. In the C-terminal domain, JNK1 has an insertion after the helix αG. This insertion consists of two helices (α1L14 and α2L14) that are common to all members of the MAPK family.	RESULTS
+133	135	αG	structure_element	As a result, the buried solvent-accessible surface area is ∼1,315 Å. In the C-terminal domain, JNK1 has an insertion after the helix αG. This insertion consists of two helices (α1L14 and α2L14) that are common to all members of the MAPK family.	RESULTS
+168	175	helices	structure_element	As a result, the buried solvent-accessible surface area is ∼1,315 Å. In the C-terminal domain, JNK1 has an insertion after the helix αG. This insertion consists of two helices (α1L14 and α2L14) that are common to all members of the MAPK family.	RESULTS
+177	182	α1L14	structure_element	As a result, the buried solvent-accessible surface area is ∼1,315 Å. In the C-terminal domain, JNK1 has an insertion after the helix αG. This insertion consists of two helices (α1L14 and α2L14) that are common to all members of the MAPK family.	RESULTS
+187	192	α2L14	structure_element	As a result, the buried solvent-accessible surface area is ∼1,315 Å. In the C-terminal domain, JNK1 has an insertion after the helix αG. This insertion consists of two helices (α1L14 and α2L14) that are common to all members of the MAPK family.	RESULTS
+232	243	MAPK family	protein_type	As a result, the buried solvent-accessible surface area is ∼1,315 Å. In the C-terminal domain, JNK1 has an insertion after the helix αG. This insertion consists of two helices (α1L14 and α2L14) that are common to all members of the MAPK family.	RESULTS
+4	23	interactive surface	site	The interactive surface in JNK1, formed by the helices αG and α2L14, displays a hydrophobic region, centred at Trp234 (Fig. 3d).	RESULTS
+27	31	JNK1	protein	The interactive surface in JNK1, formed by the helices αG and α2L14, displays a hydrophobic region, centred at Trp234 (Fig. 3d).	RESULTS
+47	54	helices	structure_element	The interactive surface in JNK1, formed by the helices αG and α2L14, displays a hydrophobic region, centred at Trp234 (Fig. 3d).	RESULTS
+55	57	αG	structure_element	The interactive surface in JNK1, formed by the helices αG and α2L14, displays a hydrophobic region, centred at Trp234 (Fig. 3d).	RESULTS
+62	67	α2L14	structure_element	The interactive surface in JNK1, formed by the helices αG and α2L14, displays a hydrophobic region, centred at Trp234 (Fig. 3d).	RESULTS
+80	98	hydrophobic region	site	The interactive surface in JNK1, formed by the helices αG and α2L14, displays a hydrophobic region, centred at Trp234 (Fig. 3d).	RESULTS
+111	117	Trp234	residue_name_number	The interactive surface in JNK1, formed by the helices αG and α2L14, displays a hydrophobic region, centred at Trp234 (Fig. 3d).	RESULTS
+4	23	MKP7-docking region	site	The MKP7-docking region includes two helices, α4 and α5, and the general acid loop.	RESULTS
+37	44	helices	structure_element	The MKP7-docking region includes two helices, α4 and α5, and the general acid loop.	RESULTS
+46	48	α4	structure_element	The MKP7-docking region includes two helices, α4 and α5, and the general acid loop.	RESULTS
+53	55	α5	structure_element	The MKP7-docking region includes two helices, α4 and α5, and the general acid loop.	RESULTS
+65	82	general acid loop	structure_element	The MKP7-docking region includes two helices, α4 and α5, and the general acid loop.	RESULTS
+21	27	Phe285	residue_name_number	The aromatic ring of Phe285 on MKP7 α5-helix is nestled in a hydrophobic pocket on JNK1, formed by side chains of Ile197, Leu198, Ile231, Trp234, Val256, Tyr259, Val260 and the aliphatic portion of His230 (Fig. 3d,f and Supplementary Fig. 1g).	RESULTS
+31	35	MKP7	protein	The aromatic ring of Phe285 on MKP7 α5-helix is nestled in a hydrophobic pocket on JNK1, formed by side chains of Ile197, Leu198, Ile231, Trp234, Val256, Tyr259, Val260 and the aliphatic portion of His230 (Fig. 3d,f and Supplementary Fig. 1g).	RESULTS
+36	44	α5-helix	structure_element	The aromatic ring of Phe285 on MKP7 α5-helix is nestled in a hydrophobic pocket on JNK1, formed by side chains of Ile197, Leu198, Ile231, Trp234, Val256, Tyr259, Val260 and the aliphatic portion of His230 (Fig. 3d,f and Supplementary Fig. 1g).	RESULTS
+61	79	hydrophobic pocket	site	The aromatic ring of Phe285 on MKP7 α5-helix is nestled in a hydrophobic pocket on JNK1, formed by side chains of Ile197, Leu198, Ile231, Trp234, Val256, Tyr259, Val260 and the aliphatic portion of His230 (Fig. 3d,f and Supplementary Fig. 1g).	RESULTS
+83	87	JNK1	protein	The aromatic ring of Phe285 on MKP7 α5-helix is nestled in a hydrophobic pocket on JNK1, formed by side chains of Ile197, Leu198, Ile231, Trp234, Val256, Tyr259, Val260 and the aliphatic portion of His230 (Fig. 3d,f and Supplementary Fig. 1g).	RESULTS
+114	120	Ile197	residue_name_number	The aromatic ring of Phe285 on MKP7 α5-helix is nestled in a hydrophobic pocket on JNK1, formed by side chains of Ile197, Leu198, Ile231, Trp234, Val256, Tyr259, Val260 and the aliphatic portion of His230 (Fig. 3d,f and Supplementary Fig. 1g).	RESULTS
+122	128	Leu198	residue_name_number	The aromatic ring of Phe285 on MKP7 α5-helix is nestled in a hydrophobic pocket on JNK1, formed by side chains of Ile197, Leu198, Ile231, Trp234, Val256, Tyr259, Val260 and the aliphatic portion of His230 (Fig. 3d,f and Supplementary Fig. 1g).	RESULTS
+130	136	Ile231	residue_name_number	The aromatic ring of Phe285 on MKP7 α5-helix is nestled in a hydrophobic pocket on JNK1, formed by side chains of Ile197, Leu198, Ile231, Trp234, Val256, Tyr259, Val260 and the aliphatic portion of His230 (Fig. 3d,f and Supplementary Fig. 1g).	RESULTS
+138	144	Trp234	residue_name_number	The aromatic ring of Phe285 on MKP7 α5-helix is nestled in a hydrophobic pocket on JNK1, formed by side chains of Ile197, Leu198, Ile231, Trp234, Val256, Tyr259, Val260 and the aliphatic portion of His230 (Fig. 3d,f and Supplementary Fig. 1g).	RESULTS
+146	152	Val256	residue_name_number	The aromatic ring of Phe285 on MKP7 α5-helix is nestled in a hydrophobic pocket on JNK1, formed by side chains of Ile197, Leu198, Ile231, Trp234, Val256, Tyr259, Val260 and the aliphatic portion of His230 (Fig. 3d,f and Supplementary Fig. 1g).	RESULTS
+154	160	Tyr259	residue_name_number	The aromatic ring of Phe285 on MKP7 α5-helix is nestled in a hydrophobic pocket on JNK1, formed by side chains of Ile197, Leu198, Ile231, Trp234, Val256, Tyr259, Val260 and the aliphatic portion of His230 (Fig. 3d,f and Supplementary Fig. 1g).	RESULTS
+162	168	Val260	residue_name_number	The aromatic ring of Phe285 on MKP7 α5-helix is nestled in a hydrophobic pocket on JNK1, formed by side chains of Ile197, Leu198, Ile231, Trp234, Val256, Tyr259, Val260 and the aliphatic portion of His230 (Fig. 3d,f and Supplementary Fig. 1g).	RESULTS
+198	204	His230	residue_name_number	The aromatic ring of Phe285 on MKP7 α5-helix is nestled in a hydrophobic pocket on JNK1, formed by side chains of Ile197, Leu198, Ile231, Trp234, Val256, Tyr259, Val260 and the aliphatic portion of His230 (Fig. 3d,f and Supplementary Fig. 1g).	RESULTS
+23	37	hydrogen bonds	bond_interaction	In addition, there are hydrogen bonds between Ser282 and Asn286 of MKP7 and His230 and Thr255 of JNK1, and the main chain of Phe215 in the general acid loop of MKP7 is hydrogen-bonded to the side chain of Gln253 in JNK1.	RESULTS
+46	52	Ser282	residue_name_number	In addition, there are hydrogen bonds between Ser282 and Asn286 of MKP7 and His230 and Thr255 of JNK1, and the main chain of Phe215 in the general acid loop of MKP7 is hydrogen-bonded to the side chain of Gln253 in JNK1.	RESULTS
+57	63	Asn286	residue_name_number	In addition, there are hydrogen bonds between Ser282 and Asn286 of MKP7 and His230 and Thr255 of JNK1, and the main chain of Phe215 in the general acid loop of MKP7 is hydrogen-bonded to the side chain of Gln253 in JNK1.	RESULTS
+67	71	MKP7	protein	In addition, there are hydrogen bonds between Ser282 and Asn286 of MKP7 and His230 and Thr255 of JNK1, and the main chain of Phe215 in the general acid loop of MKP7 is hydrogen-bonded to the side chain of Gln253 in JNK1.	RESULTS
+76	82	His230	residue_name_number	In addition, there are hydrogen bonds between Ser282 and Asn286 of MKP7 and His230 and Thr255 of JNK1, and the main chain of Phe215 in the general acid loop of MKP7 is hydrogen-bonded to the side chain of Gln253 in JNK1.	RESULTS
+87	93	Thr255	residue_name_number	In addition, there are hydrogen bonds between Ser282 and Asn286 of MKP7 and His230 and Thr255 of JNK1, and the main chain of Phe215 in the general acid loop of MKP7 is hydrogen-bonded to the side chain of Gln253 in JNK1.	RESULTS
+97	101	JNK1	protein	In addition, there are hydrogen bonds between Ser282 and Asn286 of MKP7 and His230 and Thr255 of JNK1, and the main chain of Phe215 in the general acid loop of MKP7 is hydrogen-bonded to the side chain of Gln253 in JNK1.	RESULTS
+125	131	Phe215	residue_name_number	In addition, there are hydrogen bonds between Ser282 and Asn286 of MKP7 and His230 and Thr255 of JNK1, and the main chain of Phe215 in the general acid loop of MKP7 is hydrogen-bonded to the side chain of Gln253 in JNK1.	RESULTS
+139	156	general acid loop	structure_element	In addition, there are hydrogen bonds between Ser282 and Asn286 of MKP7 and His230 and Thr255 of JNK1, and the main chain of Phe215 in the general acid loop of MKP7 is hydrogen-bonded to the side chain of Gln253 in JNK1.	RESULTS
+160	164	MKP7	protein	In addition, there are hydrogen bonds between Ser282 and Asn286 of MKP7 and His230 and Thr255 of JNK1, and the main chain of Phe215 in the general acid loop of MKP7 is hydrogen-bonded to the side chain of Gln253 in JNK1.	RESULTS
+168	183	hydrogen-bonded	bond_interaction	In addition, there are hydrogen bonds between Ser282 and Asn286 of MKP7 and His230 and Thr255 of JNK1, and the main chain of Phe215 in the general acid loop of MKP7 is hydrogen-bonded to the side chain of Gln253 in JNK1.	RESULTS
+205	211	Gln253	residue_name_number	In addition, there are hydrogen bonds between Ser282 and Asn286 of MKP7 and His230 and Thr255 of JNK1, and the main chain of Phe215 in the general acid loop of MKP7 is hydrogen-bonded to the side chain of Gln253 in JNK1.	RESULTS
+215	219	JNK1	protein	In addition, there are hydrogen bonds between Ser282 and Asn286 of MKP7 and His230 and Thr255 of JNK1, and the main chain of Phe215 in the general acid loop of MKP7 is hydrogen-bonded to the side chain of Gln253 in JNK1.	RESULTS
+4	27	second interactive area	site	The second interactive area involves the α4 helix of MKP7 and charged/polar residues of JNK1 (Fig. 3e).	RESULTS
+41	49	α4 helix	structure_element	The second interactive area involves the α4 helix of MKP7 and charged/polar residues of JNK1 (Fig. 3e).	RESULTS
+53	57	MKP7	protein	The second interactive area involves the α4 helix of MKP7 and charged/polar residues of JNK1 (Fig. 3e).	RESULTS
+88	92	JNK1	protein	The second interactive area involves the α4 helix of MKP7 and charged/polar residues of JNK1 (Fig. 3e).	RESULTS
+19	25	Asp268	residue_name_number	The carboxylate of Asp268 in MKP7 forms a salt bridge with side chain of Arg263 in JNK1, and Lys275 of MKP7 forms a hydrogen bond and a salt bridge with Thr228 and Asp229 of JNK1, respectively.	RESULTS
+29	33	MKP7	protein	The carboxylate of Asp268 in MKP7 forms a salt bridge with side chain of Arg263 in JNK1, and Lys275 of MKP7 forms a hydrogen bond and a salt bridge with Thr228 and Asp229 of JNK1, respectively.	RESULTS
+42	53	salt bridge	bond_interaction	The carboxylate of Asp268 in MKP7 forms a salt bridge with side chain of Arg263 in JNK1, and Lys275 of MKP7 forms a hydrogen bond and a salt bridge with Thr228 and Asp229 of JNK1, respectively.	RESULTS
+73	79	Arg263	residue_name_number	The carboxylate of Asp268 in MKP7 forms a salt bridge with side chain of Arg263 in JNK1, and Lys275 of MKP7 forms a hydrogen bond and a salt bridge with Thr228 and Asp229 of JNK1, respectively.	RESULTS
+83	87	JNK1	protein	The carboxylate of Asp268 in MKP7 forms a salt bridge with side chain of Arg263 in JNK1, and Lys275 of MKP7 forms a hydrogen bond and a salt bridge with Thr228 and Asp229 of JNK1, respectively.	RESULTS
+93	99	Lys275	residue_name_number	The carboxylate of Asp268 in MKP7 forms a salt bridge with side chain of Arg263 in JNK1, and Lys275 of MKP7 forms a hydrogen bond and a salt bridge with Thr228 and Asp229 of JNK1, respectively.	RESULTS
+103	107	MKP7	protein	The carboxylate of Asp268 in MKP7 forms a salt bridge with side chain of Arg263 in JNK1, and Lys275 of MKP7 forms a hydrogen bond and a salt bridge with Thr228 and Asp229 of JNK1, respectively.	RESULTS
+116	129	hydrogen bond	bond_interaction	The carboxylate of Asp268 in MKP7 forms a salt bridge with side chain of Arg263 in JNK1, and Lys275 of MKP7 forms a hydrogen bond and a salt bridge with Thr228 and Asp229 of JNK1, respectively.	RESULTS
+136	147	salt bridge	bond_interaction	The carboxylate of Asp268 in MKP7 forms a salt bridge with side chain of Arg263 in JNK1, and Lys275 of MKP7 forms a hydrogen bond and a salt bridge with Thr228 and Asp229 of JNK1, respectively.	RESULTS
+153	159	Thr228	residue_name_number	The carboxylate of Asp268 in MKP7 forms a salt bridge with side chain of Arg263 in JNK1, and Lys275 of MKP7 forms a hydrogen bond and a salt bridge with Thr228 and Asp229 of JNK1, respectively.	RESULTS
+164	170	Asp229	residue_name_number	The carboxylate of Asp268 in MKP7 forms a salt bridge with side chain of Arg263 in JNK1, and Lys275 of MKP7 forms a hydrogen bond and a salt bridge with Thr228 and Asp229 of JNK1, respectively.	RESULTS
+174	178	JNK1	protein	The carboxylate of Asp268 in MKP7 forms a salt bridge with side chain of Arg263 in JNK1, and Lys275 of MKP7 forms a hydrogen bond and a salt bridge with Thr228 and Asp229 of JNK1, respectively.	RESULTS
+0	19	Mutational analysis	experimental_method	Mutational analysis of the JNK1–MKP7 docking interface	RESULTS
+27	54	JNK1–MKP7 docking interface	site	Mutational analysis of the JNK1–MKP7 docking interface	RESULTS
+86	101	point mutations	experimental_method	To assess the importance of the aforementioned interactions, we generated a series of point mutations on the MKP7-CD and examined their effect on the MKP7-catalysed JNK1 dephosphorylation (Fig. 4a).	RESULTS
+109	113	MKP7	protein	To assess the importance of the aforementioned interactions, we generated a series of point mutations on the MKP7-CD and examined their effect on the MKP7-catalysed JNK1 dephosphorylation (Fig. 4a).	RESULTS
+114	116	CD	structure_element	To assess the importance of the aforementioned interactions, we generated a series of point mutations on the MKP7-CD and examined their effect on the MKP7-catalysed JNK1 dephosphorylation (Fig. 4a).	RESULTS
+150	154	MKP7	protein	To assess the importance of the aforementioned interactions, we generated a series of point mutations on the MKP7-CD and examined their effect on the MKP7-catalysed JNK1 dephosphorylation (Fig. 4a).	RESULTS
+165	169	JNK1	protein	To assess the importance of the aforementioned interactions, we generated a series of point mutations on the MKP7-CD and examined their effect on the MKP7-catalysed JNK1 dephosphorylation (Fig. 4a).	RESULTS
+170	187	dephosphorylation	ptm	To assess the importance of the aforementioned interactions, we generated a series of point mutations on the MKP7-CD and examined their effect on the MKP7-catalysed JNK1 dephosphorylation (Fig. 4a).	RESULTS
+30	36	Phe285	residue_name_number	When the hydrophobic residues Phe285 and Phe287 on the α5 of MKP7-CD were replaced by Asp or Ala, their phosphatase activities for JNK1 dephosphorylation decreased ∼10-fold.	RESULTS
+41	47	Phe287	residue_name_number	When the hydrophobic residues Phe285 and Phe287 on the α5 of MKP7-CD were replaced by Asp or Ala, their phosphatase activities for JNK1 dephosphorylation decreased ∼10-fold.	RESULTS
+55	57	α5	structure_element	When the hydrophobic residues Phe285 and Phe287 on the α5 of MKP7-CD were replaced by Asp or Ala, their phosphatase activities for JNK1 dephosphorylation decreased ∼10-fold.	RESULTS
+61	65	MKP7	protein	When the hydrophobic residues Phe285 and Phe287 on the α5 of MKP7-CD were replaced by Asp or Ala, their phosphatase activities for JNK1 dephosphorylation decreased ∼10-fold.	RESULTS
+66	68	CD	structure_element	When the hydrophobic residues Phe285 and Phe287 on the α5 of MKP7-CD were replaced by Asp or Ala, their phosphatase activities for JNK1 dephosphorylation decreased ∼10-fold.	RESULTS
+74	82	replaced	experimental_method	When the hydrophobic residues Phe285 and Phe287 on the α5 of MKP7-CD were replaced by Asp or Ala, their phosphatase activities for JNK1 dephosphorylation decreased ∼10-fold.	RESULTS
+86	89	Asp	residue_name	When the hydrophobic residues Phe285 and Phe287 on the α5 of MKP7-CD were replaced by Asp or Ala, their phosphatase activities for JNK1 dephosphorylation decreased ∼10-fold.	RESULTS
+93	96	Ala	residue_name	When the hydrophobic residues Phe285 and Phe287 on the α5 of MKP7-CD were replaced by Asp or Ala, their phosphatase activities for JNK1 dephosphorylation decreased ∼10-fold.	RESULTS
+131	135	JNK1	protein	When the hydrophobic residues Phe285 and Phe287 on the α5 of MKP7-CD were replaced by Asp or Ala, their phosphatase activities for JNK1 dephosphorylation decreased ∼10-fold.	RESULTS
+136	153	dephosphorylation	ptm	When the hydrophobic residues Phe285 and Phe287 on the α5 of MKP7-CD were replaced by Asp or Ala, their phosphatase activities for JNK1 dephosphorylation decreased ∼10-fold.	RESULTS
+15	26	replacement	experimental_method	In comparison, replacement of the other residues (Phe215, Asp268, Lys275, Ser282, Asn286 and Leu292) with an Ala or Asp individually led to a modest decrease in catalytic efficiencies, suggesting that this position may only affect some selectivity of MKP.	RESULTS
+50	56	Phe215	residue_name_number	In comparison, replacement of the other residues (Phe215, Asp268, Lys275, Ser282, Asn286 and Leu292) with an Ala or Asp individually led to a modest decrease in catalytic efficiencies, suggesting that this position may only affect some selectivity of MKP.	RESULTS
+58	64	Asp268	residue_name_number	In comparison, replacement of the other residues (Phe215, Asp268, Lys275, Ser282, Asn286 and Leu292) with an Ala or Asp individually led to a modest decrease in catalytic efficiencies, suggesting that this position may only affect some selectivity of MKP.	RESULTS
+66	72	Lys275	residue_name_number	In comparison, replacement of the other residues (Phe215, Asp268, Lys275, Ser282, Asn286 and Leu292) with an Ala or Asp individually led to a modest decrease in catalytic efficiencies, suggesting that this position may only affect some selectivity of MKP.	RESULTS
+74	80	Ser282	residue_name_number	In comparison, replacement of the other residues (Phe215, Asp268, Lys275, Ser282, Asn286 and Leu292) with an Ala or Asp individually led to a modest decrease in catalytic efficiencies, suggesting that this position may only affect some selectivity of MKP.	RESULTS
+82	88	Asn286	residue_name_number	In comparison, replacement of the other residues (Phe215, Asp268, Lys275, Ser282, Asn286 and Leu292) with an Ala or Asp individually led to a modest decrease in catalytic efficiencies, suggesting that this position may only affect some selectivity of MKP.	RESULTS
+93	99	Leu292	residue_name_number	In comparison, replacement of the other residues (Phe215, Asp268, Lys275, Ser282, Asn286 and Leu292) with an Ala or Asp individually led to a modest decrease in catalytic efficiencies, suggesting that this position may only affect some selectivity of MKP.	RESULTS
+109	112	Ala	residue_name	In comparison, replacement of the other residues (Phe215, Asp268, Lys275, Ser282, Asn286 and Leu292) with an Ala or Asp individually led to a modest decrease in catalytic efficiencies, suggesting that this position may only affect some selectivity of MKP.	RESULTS
+116	119	Asp	residue_name	In comparison, replacement of the other residues (Phe215, Asp268, Lys275, Ser282, Asn286 and Leu292) with an Ala or Asp individually led to a modest decrease in catalytic efficiencies, suggesting that this position may only affect some selectivity of MKP.	RESULTS
+251	254	MKP	protein_type	In comparison, replacement of the other residues (Phe215, Asp268, Lys275, Ser282, Asn286 and Leu292) with an Ala or Asp individually led to a modest decrease in catalytic efficiencies, suggesting that this position may only affect some selectivity of MKP.	RESULTS
+0	8	Mutation	experimental_method	Mutation of Leu288 markedly reduced its solubility when expressed in Escherichia coli, resulting in the insoluble aggregation of the mutant protein.	RESULTS
+12	18	Leu288	residue_name_number	Mutation of Leu288 markedly reduced its solubility when expressed in Escherichia coli, resulting in the insoluble aggregation of the mutant protein.	RESULTS
+69	85	Escherichia coli	species	Mutation of Leu288 markedly reduced its solubility when expressed in Escherichia coli, resulting in the insoluble aggregation of the mutant protein.	RESULTS
+133	139	mutant	protein_state	Mutation of Leu288 markedly reduced its solubility when expressed in Escherichia coli, resulting in the insoluble aggregation of the mutant protein.	RESULTS
+0	23	Gel filtration analysis	experimental_method	Gel filtration analysis further confirmed the key role of Phe285 in the MKP7–JNK1 interaction: no F285D–JNK1 complex was detected when 3 molar equivalents of MKP7-CD (F285D) were mixed with 1 molar equivalent of JNK1 (Fig. 4b).	RESULTS
+58	64	Phe285	residue_name_number	Gel filtration analysis further confirmed the key role of Phe285 in the MKP7–JNK1 interaction: no F285D–JNK1 complex was detected when 3 molar equivalents of MKP7-CD (F285D) were mixed with 1 molar equivalent of JNK1 (Fig. 4b).	RESULTS
+72	76	MKP7	protein	Gel filtration analysis further confirmed the key role of Phe285 in the MKP7–JNK1 interaction: no F285D–JNK1 complex was detected when 3 molar equivalents of MKP7-CD (F285D) were mixed with 1 molar equivalent of JNK1 (Fig. 4b).	RESULTS
+77	81	JNK1	protein	Gel filtration analysis further confirmed the key role of Phe285 in the MKP7–JNK1 interaction: no F285D–JNK1 complex was detected when 3 molar equivalents of MKP7-CD (F285D) were mixed with 1 molar equivalent of JNK1 (Fig. 4b).	RESULTS
+98	108	F285D–JNK1	complex_assembly	Gel filtration analysis further confirmed the key role of Phe285 in the MKP7–JNK1 interaction: no F285D–JNK1 complex was detected when 3 molar equivalents of MKP7-CD (F285D) were mixed with 1 molar equivalent of JNK1 (Fig. 4b).	RESULTS
+158	162	MKP7	protein	Gel filtration analysis further confirmed the key role of Phe285 in the MKP7–JNK1 interaction: no F285D–JNK1 complex was detected when 3 molar equivalents of MKP7-CD (F285D) were mixed with 1 molar equivalent of JNK1 (Fig. 4b).	RESULTS
+163	165	CD	structure_element	Gel filtration analysis further confirmed the key role of Phe285 in the MKP7–JNK1 interaction: no F285D–JNK1 complex was detected when 3 molar equivalents of MKP7-CD (F285D) were mixed with 1 molar equivalent of JNK1 (Fig. 4b).	RESULTS
+167	172	F285D	mutant	Gel filtration analysis further confirmed the key role of Phe285 in the MKP7–JNK1 interaction: no F285D–JNK1 complex was detected when 3 molar equivalents of MKP7-CD (F285D) were mixed with 1 molar equivalent of JNK1 (Fig. 4b).	RESULTS
+212	216	JNK1	protein	Gel filtration analysis further confirmed the key role of Phe285 in the MKP7–JNK1 interaction: no F285D–JNK1 complex was detected when 3 molar equivalents of MKP7-CD (F285D) were mixed with 1 molar equivalent of JNK1 (Fig. 4b).	RESULTS
+15	23	mutation	experimental_method	Interestingly, mutation of Phe287 results in a considerable loss of activity against pJNK1 without altering the affinity of MKP7-CD for JNK1 (Supplementary Fig. 2a).	RESULTS
+27	33	Phe287	residue_name_number	Interestingly, mutation of Phe287 results in a considerable loss of activity against pJNK1 without altering the affinity of MKP7-CD for JNK1 (Supplementary Fig. 2a).	RESULTS
+85	86	p	protein_state	Interestingly, mutation of Phe287 results in a considerable loss of activity against pJNK1 without altering the affinity of MKP7-CD for JNK1 (Supplementary Fig. 2a).	RESULTS
+86	90	JNK1	protein	Interestingly, mutation of Phe287 results in a considerable loss of activity against pJNK1 without altering the affinity of MKP7-CD for JNK1 (Supplementary Fig. 2a).	RESULTS
+112	120	affinity	evidence	Interestingly, mutation of Phe287 results in a considerable loss of activity against pJNK1 without altering the affinity of MKP7-CD for JNK1 (Supplementary Fig. 2a).	RESULTS
+124	128	MKP7	protein	Interestingly, mutation of Phe287 results in a considerable loss of activity against pJNK1 without altering the affinity of MKP7-CD for JNK1 (Supplementary Fig. 2a).	RESULTS
+129	131	CD	structure_element	Interestingly, mutation of Phe287 results in a considerable loss of activity against pJNK1 without altering the affinity of MKP7-CD for JNK1 (Supplementary Fig. 2a).	RESULTS
+136	140	JNK1	protein	Interestingly, mutation of Phe287 results in a considerable loss of activity against pJNK1 without altering the affinity of MKP7-CD for JNK1 (Supplementary Fig. 2a).	RESULTS
+30	45	point mutations	experimental_method	We also generated a series of point mutations in the JNK1 and assessed the effect on JNK1 binding using the GST pull-down assay (Fig. 4c).	RESULTS
+53	57	JNK1	protein	We also generated a series of point mutations in the JNK1 and assessed the effect on JNK1 binding using the GST pull-down assay (Fig. 4c).	RESULTS
+85	89	JNK1	protein	We also generated a series of point mutations in the JNK1 and assessed the effect on JNK1 binding using the GST pull-down assay (Fig. 4c).	RESULTS
+108	127	GST pull-down assay	experimental_method	We also generated a series of point mutations in the JNK1 and assessed the effect on JNK1 binding using the GST pull-down assay (Fig. 4c).	RESULTS
+0	12	Substitution	experimental_method	Substitution at Asp229, Trp234, Thr255, Val256, Tyr259 and Val260 significantly reduced the binding affinity of MKP7-CD for JNK.	RESULTS
+16	22	Asp229	residue_name_number	Substitution at Asp229, Trp234, Thr255, Val256, Tyr259 and Val260 significantly reduced the binding affinity of MKP7-CD for JNK.	RESULTS
+24	30	Trp234	residue_name_number	Substitution at Asp229, Trp234, Thr255, Val256, Tyr259 and Val260 significantly reduced the binding affinity of MKP7-CD for JNK.	RESULTS
+32	38	Thr255	residue_name_number	Substitution at Asp229, Trp234, Thr255, Val256, Tyr259 and Val260 significantly reduced the binding affinity of MKP7-CD for JNK.	RESULTS
+40	46	Val256	residue_name_number	Substitution at Asp229, Trp234, Thr255, Val256, Tyr259 and Val260 significantly reduced the binding affinity of MKP7-CD for JNK.	RESULTS
+48	54	Tyr259	residue_name_number	Substitution at Asp229, Trp234, Thr255, Val256, Tyr259 and Val260 significantly reduced the binding affinity of MKP7-CD for JNK.	RESULTS
+59	65	Val260	residue_name_number	Substitution at Asp229, Trp234, Thr255, Val256, Tyr259 and Val260 significantly reduced the binding affinity of MKP7-CD for JNK.	RESULTS
+92	108	binding affinity	evidence	Substitution at Asp229, Trp234, Thr255, Val256, Tyr259 and Val260 significantly reduced the binding affinity of MKP7-CD for JNK.	RESULTS
+112	116	MKP7	protein	Substitution at Asp229, Trp234, Thr255, Val256, Tyr259 and Val260 significantly reduced the binding affinity of MKP7-CD for JNK.	RESULTS
+117	119	CD	structure_element	Substitution at Asp229, Trp234, Thr255, Val256, Tyr259 and Val260 significantly reduced the binding affinity of MKP7-CD for JNK.	RESULTS
+124	127	JNK	protein_type	Substitution at Asp229, Trp234, Thr255, Val256, Tyr259 and Val260 significantly reduced the binding affinity of MKP7-CD for JNK.	RESULTS
+154	160	mutant	protein_state	To determine whether the deficiencies in their abilities to bind partner proteins or carry out catalytic function are owing to misfolding of the purified mutant proteins, we also examined the folding properties of the JNK1 and MKP7 mutants with circular dichroism.	RESULTS
+218	222	JNK1	protein	To determine whether the deficiencies in their abilities to bind partner proteins or carry out catalytic function are owing to misfolding of the purified mutant proteins, we also examined the folding properties of the JNK1 and MKP7 mutants with circular dichroism.	RESULTS
+227	231	MKP7	protein	To determine whether the deficiencies in their abilities to bind partner proteins or carry out catalytic function are owing to misfolding of the purified mutant proteins, we also examined the folding properties of the JNK1 and MKP7 mutants with circular dichroism.	RESULTS
+232	239	mutants	protein_state	To determine whether the deficiencies in their abilities to bind partner proteins or carry out catalytic function are owing to misfolding of the purified mutant proteins, we also examined the folding properties of the JNK1 and MKP7 mutants with circular dichroism.	RESULTS
+245	263	circular dichroism	experimental_method	To determine whether the deficiencies in their abilities to bind partner proteins or carry out catalytic function are owing to misfolding of the purified mutant proteins, we also examined the folding properties of the JNK1 and MKP7 mutants with circular dichroism.	RESULTS
+4	11	spectra	evidence	The spectra of these mutants are similar to the wild-type proteins, indicating that these mutants fold as well as the wild-type proteins (Fig. 4d,e).	RESULTS
+21	28	mutants	protein_state	The spectra of these mutants are similar to the wild-type proteins, indicating that these mutants fold as well as the wild-type proteins (Fig. 4d,e).	RESULTS
+48	57	wild-type	protein_state	The spectra of these mutants are similar to the wild-type proteins, indicating that these mutants fold as well as the wild-type proteins (Fig. 4d,e).	RESULTS
+90	97	mutants	protein_state	The spectra of these mutants are similar to the wild-type proteins, indicating that these mutants fold as well as the wild-type proteins (Fig. 4d,e).	RESULTS
+118	127	wild-type	protein_state	The spectra of these mutants are similar to the wild-type proteins, indicating that these mutants fold as well as the wild-type proteins (Fig. 4d,e).	RESULTS
+62	84	crystallographic model	evidence	Taken together, these results are consistent with the present crystallographic model, which reveal the hydrophobic contacts between the MKP7 catalytic domain and JNK1 have a predominant role in the enzyme–substrate interaction, and hydrophobic residue Phe285 in the MKP7-CD is a key residue for its high-affinity binding to JNK1.	RESULTS
+103	123	hydrophobic contacts	bond_interaction	Taken together, these results are consistent with the present crystallographic model, which reveal the hydrophobic contacts between the MKP7 catalytic domain and JNK1 have a predominant role in the enzyme–substrate interaction, and hydrophobic residue Phe285 in the MKP7-CD is a key residue for its high-affinity binding to JNK1.	RESULTS
+136	140	MKP7	protein	Taken together, these results are consistent with the present crystallographic model, which reveal the hydrophobic contacts between the MKP7 catalytic domain and JNK1 have a predominant role in the enzyme–substrate interaction, and hydrophobic residue Phe285 in the MKP7-CD is a key residue for its high-affinity binding to JNK1.	RESULTS
+141	157	catalytic domain	structure_element	Taken together, these results are consistent with the present crystallographic model, which reveal the hydrophobic contacts between the MKP7 catalytic domain and JNK1 have a predominant role in the enzyme–substrate interaction, and hydrophobic residue Phe285 in the MKP7-CD is a key residue for its high-affinity binding to JNK1.	RESULTS
+162	166	JNK1	protein	Taken together, these results are consistent with the present crystallographic model, which reveal the hydrophobic contacts between the MKP7 catalytic domain and JNK1 have a predominant role in the enzyme–substrate interaction, and hydrophobic residue Phe285 in the MKP7-CD is a key residue for its high-affinity binding to JNK1.	RESULTS
+252	258	Phe285	residue_name_number	Taken together, these results are consistent with the present crystallographic model, which reveal the hydrophobic contacts between the MKP7 catalytic domain and JNK1 have a predominant role in the enzyme–substrate interaction, and hydrophobic residue Phe285 in the MKP7-CD is a key residue for its high-affinity binding to JNK1.	RESULTS
+266	270	MKP7	protein	Taken together, these results are consistent with the present crystallographic model, which reveal the hydrophobic contacts between the MKP7 catalytic domain and JNK1 have a predominant role in the enzyme–substrate interaction, and hydrophobic residue Phe285 in the MKP7-CD is a key residue for its high-affinity binding to JNK1.	RESULTS
+271	273	CD	structure_element	Taken together, these results are consistent with the present crystallographic model, which reveal the hydrophobic contacts between the MKP7 catalytic domain and JNK1 have a predominant role in the enzyme–substrate interaction, and hydrophobic residue Phe285 in the MKP7-CD is a key residue for its high-affinity binding to JNK1.	RESULTS
+324	328	JNK1	protein	Taken together, these results are consistent with the present crystallographic model, which reveal the hydrophobic contacts between the MKP7 catalytic domain and JNK1 have a predominant role in the enzyme–substrate interaction, and hydrophobic residue Phe285 in the MKP7-CD is a key residue for its high-affinity binding to JNK1.	RESULTS
+77	81	MKPs	protein_type	It has previously been reported that several cytosolic and inducible nuclear MKPs undergo catalytic activation upon interaction with the MAPK substrates.	RESULTS
+137	141	MAPK	protein_type	It has previously been reported that several cytosolic and inducible nuclear MKPs undergo catalytic activation upon interaction with the MAPK substrates.	RESULTS
+30	34	MKP3	protein	This allosteric activation of MKP3 has been well-documented in vitro using pNPP, a small-molecule phosphotyrosine analogue of its normal substrate.	RESULTS
+75	79	pNPP	chemical	This allosteric activation of MKP3 has been well-documented in vitro using pNPP, a small-molecule phosphotyrosine analogue of its normal substrate.	RESULTS
+98	113	phosphotyrosine	residue_name	This allosteric activation of MKP3 has been well-documented in vitro using pNPP, a small-molecule phosphotyrosine analogue of its normal substrate.	RESULTS
+16	23	pNPPase	protein_type	We then assayed pNPPase activities of MKP7ΔC304 and MKP7-CD in the presence of JNK1.	RESULTS
+38	47	MKP7ΔC304	mutant	We then assayed pNPPase activities of MKP7ΔC304 and MKP7-CD in the presence of JNK1.	RESULTS
+52	56	MKP7	protein	We then assayed pNPPase activities of MKP7ΔC304 and MKP7-CD in the presence of JNK1.	RESULTS
+57	59	CD	structure_element	We then assayed pNPPase activities of MKP7ΔC304 and MKP7-CD in the presence of JNK1.	RESULTS
+67	78	presence of	protein_state	We then assayed pNPPase activities of MKP7ΔC304 and MKP7-CD in the presence of JNK1.	RESULTS
+79	83	JNK1	protein	We then assayed pNPPase activities of MKP7ΔC304 and MKP7-CD in the presence of JNK1.	RESULTS
+0	10	Incubation	experimental_method	Incubation of MKP7 with JNK1 did not markedly stimulate the phosphatase activity, which is consistent with previous results that MKP7 solely possesses the intrinsic activity (Supplementary Fig. 2b).	RESULTS
+14	18	MKP7	protein	Incubation of MKP7 with JNK1 did not markedly stimulate the phosphatase activity, which is consistent with previous results that MKP7 solely possesses the intrinsic activity (Supplementary Fig. 2b).	RESULTS
+24	28	JNK1	protein	Incubation of MKP7 with JNK1 did not markedly stimulate the phosphatase activity, which is consistent with previous results that MKP7 solely possesses the intrinsic activity (Supplementary Fig. 2b).	RESULTS
+60	71	phosphatase	protein_type	Incubation of MKP7 with JNK1 did not markedly stimulate the phosphatase activity, which is consistent with previous results that MKP7 solely possesses the intrinsic activity (Supplementary Fig. 2b).	RESULTS
+129	133	MKP7	protein	Incubation of MKP7 with JNK1 did not markedly stimulate the phosphatase activity, which is consistent with previous results that MKP7 solely possesses the intrinsic activity (Supplementary Fig. 2b).	RESULTS
+10	14	pNPP	chemical	The small pNPP molecule binds directly at the enzyme active site and can be used to probe the reaction mechanism of protein phosphatases.	RESULTS
+53	64	active site	site	The small pNPP molecule binds directly at the enzyme active site and can be used to probe the reaction mechanism of protein phosphatases.	RESULTS
+116	136	protein phosphatases	protein_type	The small pNPP molecule binds directly at the enzyme active site and can be used to probe the reaction mechanism of protein phosphatases.	RESULTS
+41	45	MKP7	protein	We therefore examined the effects of the MKP7-CD mutants on their pNPPase activities.	RESULTS
+46	48	CD	structure_element	We therefore examined the effects of the MKP7-CD mutants on their pNPPase activities.	RESULTS
+49	56	mutants	protein_state	We therefore examined the effects of the MKP7-CD mutants on their pNPPase activities.	RESULTS
+66	73	pNPPase	protein_type	We therefore examined the effects of the MKP7-CD mutants on their pNPPase activities.	RESULTS
+29	36	mutants	protein_state	As shown in Fig. 4f, all the mutants, except F287D/A, showed little or no activity change compared with the wild-type MKP7-CD.	RESULTS
+45	52	F287D/A	mutant	As shown in Fig. 4f, all the mutants, except F287D/A, showed little or no activity change compared with the wild-type MKP7-CD.	RESULTS
+108	117	wild-type	protein_state	As shown in Fig. 4f, all the mutants, except F287D/A, showed little or no activity change compared with the wild-type MKP7-CD.	RESULTS
+118	122	MKP7	protein	As shown in Fig. 4f, all the mutants, except F287D/A, showed little or no activity change compared with the wild-type MKP7-CD.	RESULTS
+123	125	CD	structure_element	As shown in Fig. 4f, all the mutants, except F287D/A, showed little or no activity change compared with the wild-type MKP7-CD.	RESULTS
+7	19	JNK1/MKP7-CD	complex_assembly	In the JNK1/MKP7-CD complex structure, Phe287 of MKP7 does not make contacts with JNK1 substrate.	RESULTS
+28	37	structure	evidence	In the JNK1/MKP7-CD complex structure, Phe287 of MKP7 does not make contacts with JNK1 substrate.	RESULTS
+39	45	Phe287	residue_name_number	In the JNK1/MKP7-CD complex structure, Phe287 of MKP7 does not make contacts with JNK1 substrate.	RESULTS
+49	53	MKP7	protein	In the JNK1/MKP7-CD complex structure, Phe287 of MKP7 does not make contacts with JNK1 substrate.	RESULTS
+82	86	JNK1	protein	In the JNK1/MKP7-CD complex structure, Phe287 of MKP7 does not make contacts with JNK1 substrate.	RESULTS
+21	27	pocket	site	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+56	62	P-loop	structure_element	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+67	84	general acid loop	structure_element	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+95	115	hydrophobic contacts	bond_interaction	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+162	168	Arg250	residue_name_number	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+170	176	Glu217	residue_name_number	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+181	187	Ile219	residue_name_number	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+205	211	Phe287	residue_name_number	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+215	219	MKP7	protein	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+291	295	PTPs	protein_type	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+297	303	Gln266	residue_name_number	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+307	312	PTP1B	protein	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+318	321	VHR	protein	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+323	329	Phe166	residue_name_number	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+333	336	VHR	protein	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+366	386	active-site residues	site	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+390	394	MKP7	protein	It penetrates into a pocket formed by residues from the P-loop and general acid loop and forms hydrophobic contacts with the aliphatic portions of side chains of Arg250, Glu217 and Ile219, suggesting that Phe287 in MKP7 would play a similar role to that of its structural counterpart in the PTPs (Gln266 in PTP1B) and VHR (Phe166 in VHR) in the precise alignment of active-site residues in MKP7 with respect to the substrate for efficient catalysis (Supplementary Fig. 2c).	RESULTS
+0	29	Kinase-associated phosphatase	protein	Kinase-associated phosphatase (KAP), a member of the DUSP family, plays a crucial role in cell cycle regulation by dephosphorylating the pThr160 residue of CDK2 (cyclin-dependent kinase 2).	RESULTS
+31	34	KAP	protein	Kinase-associated phosphatase (KAP), a member of the DUSP family, plays a crucial role in cell cycle regulation by dephosphorylating the pThr160 residue of CDK2 (cyclin-dependent kinase 2).	RESULTS
+53	64	DUSP family	protein_type	Kinase-associated phosphatase (KAP), a member of the DUSP family, plays a crucial role in cell cycle regulation by dephosphorylating the pThr160 residue of CDK2 (cyclin-dependent kinase 2).	RESULTS
+137	144	pThr160	ptm	Kinase-associated phosphatase (KAP), a member of the DUSP family, plays a crucial role in cell cycle regulation by dephosphorylating the pThr160 residue of CDK2 (cyclin-dependent kinase 2).	RESULTS
+156	160	CDK2	protein	Kinase-associated phosphatase (KAP), a member of the DUSP family, plays a crucial role in cell cycle regulation by dephosphorylating the pThr160 residue of CDK2 (cyclin-dependent kinase 2).	RESULTS
+162	187	cyclin-dependent kinase 2	protein	Kinase-associated phosphatase (KAP), a member of the DUSP family, plays a crucial role in cell cycle regulation by dephosphorylating the pThr160 residue of CDK2 (cyclin-dependent kinase 2).	RESULTS
+4	21	crystal structure	evidence	The crystal structure of the CDK2/KAP complex has been determined at 3.0 Å (Fig. 5a).	RESULTS
+29	37	CDK2/KAP	complex_assembly	The crystal structure of the CDK2/KAP complex has been determined at 3.0 Å (Fig. 5a).	RESULTS
+4	13	interface	site	The interface between these two proteins consists of three discontinuous contact regions.	RESULTS
+72	75	KAP	protein	Biochemical results suggested that the affinity and specificity between KAP and CDK2 results from the recognition site comprising CDK2 residues from the αG helix and L14 loop and the N-terminal helical region of KAP (Fig. 5b).	RESULTS
+80	84	CDK2	protein	Biochemical results suggested that the affinity and specificity between KAP and CDK2 results from the recognition site comprising CDK2 residues from the αG helix and L14 loop and the N-terminal helical region of KAP (Fig. 5b).	RESULTS
+102	118	recognition site	site	Biochemical results suggested that the affinity and specificity between KAP and CDK2 results from the recognition site comprising CDK2 residues from the αG helix and L14 loop and the N-terminal helical region of KAP (Fig. 5b).	RESULTS
+130	134	CDK2	protein	Biochemical results suggested that the affinity and specificity between KAP and CDK2 results from the recognition site comprising CDK2 residues from the αG helix and L14 loop and the N-terminal helical region of KAP (Fig. 5b).	RESULTS
+153	161	αG helix	structure_element	Biochemical results suggested that the affinity and specificity between KAP and CDK2 results from the recognition site comprising CDK2 residues from the αG helix and L14 loop and the N-terminal helical region of KAP (Fig. 5b).	RESULTS
+166	174	L14 loop	structure_element	Biochemical results suggested that the affinity and specificity between KAP and CDK2 results from the recognition site comprising CDK2 residues from the αG helix and L14 loop and the N-terminal helical region of KAP (Fig. 5b).	RESULTS
+183	208	N-terminal helical region	structure_element	Biochemical results suggested that the affinity and specificity between KAP and CDK2 results from the recognition site comprising CDK2 residues from the αG helix and L14 loop and the N-terminal helical region of KAP (Fig. 5b).	RESULTS
+212	215	KAP	protein	Biochemical results suggested that the affinity and specificity between KAP and CDK2 results from the recognition site comprising CDK2 residues from the αG helix and L14 loop and the N-terminal helical region of KAP (Fig. 5b).	RESULTS
+11	24	hydrogen bond	bond_interaction	There is a hydrogen bond between the main-chain nitrogen of Ile183 (KAP) and side chain oxygen of Glu208 (CDK2), and salt bridges between Lys184 of KAP and Asp235 of CDK2.	RESULTS
+60	66	Ile183	residue_name_number	There is a hydrogen bond between the main-chain nitrogen of Ile183 (KAP) and side chain oxygen of Glu208 (CDK2), and salt bridges between Lys184 of KAP and Asp235 of CDK2.	RESULTS
+68	71	KAP	protein	There is a hydrogen bond between the main-chain nitrogen of Ile183 (KAP) and side chain oxygen of Glu208 (CDK2), and salt bridges between Lys184 of KAP and Asp235 of CDK2.	RESULTS
+98	104	Glu208	residue_name_number	There is a hydrogen bond between the main-chain nitrogen of Ile183 (KAP) and side chain oxygen of Glu208 (CDK2), and salt bridges between Lys184 of KAP and Asp235 of CDK2.	RESULTS
+106	110	CDK2	protein	There is a hydrogen bond between the main-chain nitrogen of Ile183 (KAP) and side chain oxygen of Glu208 (CDK2), and salt bridges between Lys184 of KAP and Asp235 of CDK2.	RESULTS
+138	144	Lys184	residue_name_number	There is a hydrogen bond between the main-chain nitrogen of Ile183 (KAP) and side chain oxygen of Glu208 (CDK2), and salt bridges between Lys184 of KAP and Asp235 of CDK2.	RESULTS
+148	151	KAP	protein	There is a hydrogen bond between the main-chain nitrogen of Ile183 (KAP) and side chain oxygen of Glu208 (CDK2), and salt bridges between Lys184 of KAP and Asp235 of CDK2.	RESULTS
+156	162	Asp235	residue_name_number	There is a hydrogen bond between the main-chain nitrogen of Ile183 (KAP) and side chain oxygen of Glu208 (CDK2), and salt bridges between Lys184 of KAP and Asp235 of CDK2.	RESULTS
+166	170	CDK2	protein	There is a hydrogen bond between the main-chain nitrogen of Ile183 (KAP) and side chain oxygen of Glu208 (CDK2), and salt bridges between Lys184 of KAP and Asp235 of CDK2.	RESULTS
+0	19	Structural analysis	experimental_method	Structural analysis and sequence alignment reveal that one of the few differences between MKP7-CD and KAP in the substrate-binding region is the presence of the motif FNFL in MKP7-CD, which corresponds to IKQY in KAP (Fig. 5c).	RESULTS
+24	42	sequence alignment	experimental_method	Structural analysis and sequence alignment reveal that one of the few differences between MKP7-CD and KAP in the substrate-binding region is the presence of the motif FNFL in MKP7-CD, which corresponds to IKQY in KAP (Fig. 5c).	RESULTS
+90	94	MKP7	protein	Structural analysis and sequence alignment reveal that one of the few differences between MKP7-CD and KAP in the substrate-binding region is the presence of the motif FNFL in MKP7-CD, which corresponds to IKQY in KAP (Fig. 5c).	RESULTS
+95	97	CD	structure_element	Structural analysis and sequence alignment reveal that one of the few differences between MKP7-CD and KAP in the substrate-binding region is the presence of the motif FNFL in MKP7-CD, which corresponds to IKQY in KAP (Fig. 5c).	RESULTS
+102	105	KAP	protein	Structural analysis and sequence alignment reveal that one of the few differences between MKP7-CD and KAP in the substrate-binding region is the presence of the motif FNFL in MKP7-CD, which corresponds to IKQY in KAP (Fig. 5c).	RESULTS
+113	137	substrate-binding region	site	Structural analysis and sequence alignment reveal that one of the few differences between MKP7-CD and KAP in the substrate-binding region is the presence of the motif FNFL in MKP7-CD, which corresponds to IKQY in KAP (Fig. 5c).	RESULTS
+167	171	FNFL	structure_element	Structural analysis and sequence alignment reveal that one of the few differences between MKP7-CD and KAP in the substrate-binding region is the presence of the motif FNFL in MKP7-CD, which corresponds to IKQY in KAP (Fig. 5c).	RESULTS
+175	179	MKP7	protein	Structural analysis and sequence alignment reveal that one of the few differences between MKP7-CD and KAP in the substrate-binding region is the presence of the motif FNFL in MKP7-CD, which corresponds to IKQY in KAP (Fig. 5c).	RESULTS
+180	182	CD	structure_element	Structural analysis and sequence alignment reveal that one of the few differences between MKP7-CD and KAP in the substrate-binding region is the presence of the motif FNFL in MKP7-CD, which corresponds to IKQY in KAP (Fig. 5c).	RESULTS
+205	209	IKQY	structure_element	Structural analysis and sequence alignment reveal that one of the few differences between MKP7-CD and KAP in the substrate-binding region is the presence of the motif FNFL in MKP7-CD, which corresponds to IKQY in KAP (Fig. 5c).	RESULTS
+213	216	KAP	protein	Structural analysis and sequence alignment reveal that one of the few differences between MKP7-CD and KAP in the substrate-binding region is the presence of the motif FNFL in MKP7-CD, which corresponds to IKQY in KAP (Fig. 5c).	RESULTS
+4	16	substitution	experimental_method	The substitution of the two hydrophobic residues with charged/polar residues (F285I/N286K) seriously disrupts the hydrophobic interaction required for MKP7 binding on JNK1 (Fig. 4a).	RESULTS
+78	83	F285I	mutant	The substitution of the two hydrophobic residues with charged/polar residues (F285I/N286K) seriously disrupts the hydrophobic interaction required for MKP7 binding on JNK1 (Fig. 4a).	RESULTS
+84	89	N286K	mutant	The substitution of the two hydrophobic residues with charged/polar residues (F285I/N286K) seriously disrupts the hydrophobic interaction required for MKP7 binding on JNK1 (Fig. 4a).	RESULTS
+114	137	hydrophobic interaction	bond_interaction	The substitution of the two hydrophobic residues with charged/polar residues (F285I/N286K) seriously disrupts the hydrophobic interaction required for MKP7 binding on JNK1 (Fig. 4a).	RESULTS
+151	155	MKP7	protein	The substitution of the two hydrophobic residues with charged/polar residues (F285I/N286K) seriously disrupts the hydrophobic interaction required for MKP7 binding on JNK1 (Fig. 4a).	RESULTS
+167	171	JNK1	protein	The substitution of the two hydrophobic residues with charged/polar residues (F285I/N286K) seriously disrupts the hydrophobic interaction required for MKP7 binding on JNK1 (Fig. 4a).	RESULTS
+13	19	His230	residue_name_number	In addition, His230 and Val256 in JNK1 are replaced by the negatively charged residues Glu208 and Asp235 in CDK2 (Fig. 5d), and the charge distribution on the CDK2 interactive surface is quite different from that of JNK.	RESULTS
+24	30	Val256	residue_name_number	In addition, His230 and Val256 in JNK1 are replaced by the negatively charged residues Glu208 and Asp235 in CDK2 (Fig. 5d), and the charge distribution on the CDK2 interactive surface is quite different from that of JNK.	RESULTS
+34	38	JNK1	protein	In addition, His230 and Val256 in JNK1 are replaced by the negatively charged residues Glu208 and Asp235 in CDK2 (Fig. 5d), and the charge distribution on the CDK2 interactive surface is quite different from that of JNK.	RESULTS
+87	93	Glu208	residue_name_number	In addition, His230 and Val256 in JNK1 are replaced by the negatively charged residues Glu208 and Asp235 in CDK2 (Fig. 5d), and the charge distribution on the CDK2 interactive surface is quite different from that of JNK.	RESULTS
+98	104	Asp235	residue_name_number	In addition, His230 and Val256 in JNK1 are replaced by the negatively charged residues Glu208 and Asp235 in CDK2 (Fig. 5d), and the charge distribution on the CDK2 interactive surface is quite different from that of JNK.	RESULTS
+108	112	CDK2	protein	In addition, His230 and Val256 in JNK1 are replaced by the negatively charged residues Glu208 and Asp235 in CDK2 (Fig. 5d), and the charge distribution on the CDK2 interactive surface is quite different from that of JNK.	RESULTS
+159	163	CDK2	protein	In addition, His230 and Val256 in JNK1 are replaced by the negatively charged residues Glu208 and Asp235 in CDK2 (Fig. 5d), and the charge distribution on the CDK2 interactive surface is quite different from that of JNK.	RESULTS
+164	183	interactive surface	site	In addition, His230 and Val256 in JNK1 are replaced by the negatively charged residues Glu208 and Asp235 in CDK2 (Fig. 5d), and the charge distribution on the CDK2 interactive surface is quite different from that of JNK.	RESULTS
+216	219	JNK	protein_type	In addition, His230 and Val256 in JNK1 are replaced by the negatively charged residues Glu208 and Asp235 in CDK2 (Fig. 5d), and the charge distribution on the CDK2 interactive surface is quite different from that of JNK.	RESULTS
+35	53	hydrophobic pocket	site	These data indicated that a unique hydrophobic pocket formed between the MAPK insert and αG helix plays a major role in the substrate recognition by MKPs.	RESULTS
+73	84	MAPK insert	structure_element	These data indicated that a unique hydrophobic pocket formed between the MAPK insert and αG helix plays a major role in the substrate recognition by MKPs.	RESULTS
+89	97	αG helix	structure_element	These data indicated that a unique hydrophobic pocket formed between the MAPK insert and αG helix plays a major role in the substrate recognition by MKPs.	RESULTS
+149	153	MKPs	protein_type	These data indicated that a unique hydrophobic pocket formed between the MAPK insert and αG helix plays a major role in the substrate recognition by MKPs.	RESULTS
+0	6	F-site	site	F-site interaction is crucial for JNK1 inactivation in vivo	RESULTS
+34	38	JNK1	protein	F-site interaction is crucial for JNK1 inactivation in vivo	RESULTS
+0	3	JNK	protein_type	JNK is activated following cellular exposure to a number of acute stimuli such as anisomycin, H2O2, ultraviolet light, sorbitol, DNA-damaging agents and several strong apoptosis inducers (etoposide, cisplatin and taxol).	RESULTS
+82	92	anisomycin	chemical	JNK is activated following cellular exposure to a number of acute stimuli such as anisomycin, H2O2, ultraviolet light, sorbitol, DNA-damaging agents and several strong apoptosis inducers (etoposide, cisplatin and taxol).	RESULTS
+94	98	H2O2	chemical	JNK is activated following cellular exposure to a number of acute stimuli such as anisomycin, H2O2, ultraviolet light, sorbitol, DNA-damaging agents and several strong apoptosis inducers (etoposide, cisplatin and taxol).	RESULTS
+119	127	sorbitol	chemical	JNK is activated following cellular exposure to a number of acute stimuli such as anisomycin, H2O2, ultraviolet light, sorbitol, DNA-damaging agents and several strong apoptosis inducers (etoposide, cisplatin and taxol).	RESULTS
+188	197	etoposide	chemical	JNK is activated following cellular exposure to a number of acute stimuli such as anisomycin, H2O2, ultraviolet light, sorbitol, DNA-damaging agents and several strong apoptosis inducers (etoposide, cisplatin and taxol).	RESULTS
+199	208	cisplatin	chemical	JNK is activated following cellular exposure to a number of acute stimuli such as anisomycin, H2O2, ultraviolet light, sorbitol, DNA-damaging agents and several strong apoptosis inducers (etoposide, cisplatin and taxol).	RESULTS
+213	218	taxol	chemical	JNK is activated following cellular exposure to a number of acute stimuli such as anisomycin, H2O2, ultraviolet light, sorbitol, DNA-damaging agents and several strong apoptosis inducers (etoposide, cisplatin and taxol).	RESULTS
+25	29	MKP7	protein	To assess the effects of MKP7 and its mutants on the activation of endogenous JNK in vivo, HEK293T cells were transfected with blank vector or with HA-tagged constructs for full-length MKP7, MKP7ΔC304 and MKP7-CD or MKP7 mutants, and stimulated with ultraviolet or etoposide treatment.	RESULTS
+38	45	mutants	protein_state	To assess the effects of MKP7 and its mutants on the activation of endogenous JNK in vivo, HEK293T cells were transfected with blank vector or with HA-tagged constructs for full-length MKP7, MKP7ΔC304 and MKP7-CD or MKP7 mutants, and stimulated with ultraviolet or etoposide treatment.	RESULTS
+78	81	JNK	protein_type	To assess the effects of MKP7 and its mutants on the activation of endogenous JNK in vivo, HEK293T cells were transfected with blank vector or with HA-tagged constructs for full-length MKP7, MKP7ΔC304 and MKP7-CD or MKP7 mutants, and stimulated with ultraviolet or etoposide treatment.	RESULTS
+148	157	HA-tagged	protein_state	To assess the effects of MKP7 and its mutants on the activation of endogenous JNK in vivo, HEK293T cells were transfected with blank vector or with HA-tagged constructs for full-length MKP7, MKP7ΔC304 and MKP7-CD or MKP7 mutants, and stimulated with ultraviolet or etoposide treatment.	RESULTS
+173	184	full-length	protein_state	To assess the effects of MKP7 and its mutants on the activation of endogenous JNK in vivo, HEK293T cells were transfected with blank vector or with HA-tagged constructs for full-length MKP7, MKP7ΔC304 and MKP7-CD or MKP7 mutants, and stimulated with ultraviolet or etoposide treatment.	RESULTS
+185	189	MKP7	protein	To assess the effects of MKP7 and its mutants on the activation of endogenous JNK in vivo, HEK293T cells were transfected with blank vector or with HA-tagged constructs for full-length MKP7, MKP7ΔC304 and MKP7-CD or MKP7 mutants, and stimulated with ultraviolet or etoposide treatment.	RESULTS
+191	200	MKP7ΔC304	mutant	To assess the effects of MKP7 and its mutants on the activation of endogenous JNK in vivo, HEK293T cells were transfected with blank vector or with HA-tagged constructs for full-length MKP7, MKP7ΔC304 and MKP7-CD or MKP7 mutants, and stimulated with ultraviolet or etoposide treatment.	RESULTS
+205	209	MKP7	protein	To assess the effects of MKP7 and its mutants on the activation of endogenous JNK in vivo, HEK293T cells were transfected with blank vector or with HA-tagged constructs for full-length MKP7, MKP7ΔC304 and MKP7-CD or MKP7 mutants, and stimulated with ultraviolet or etoposide treatment.	RESULTS
+210	212	CD	structure_element	To assess the effects of MKP7 and its mutants on the activation of endogenous JNK in vivo, HEK293T cells were transfected with blank vector or with HA-tagged constructs for full-length MKP7, MKP7ΔC304 and MKP7-CD or MKP7 mutants, and stimulated with ultraviolet or etoposide treatment.	RESULTS
+216	220	MKP7	protein	To assess the effects of MKP7 and its mutants on the activation of endogenous JNK in vivo, HEK293T cells were transfected with blank vector or with HA-tagged constructs for full-length MKP7, MKP7ΔC304 and MKP7-CD or MKP7 mutants, and stimulated with ultraviolet or etoposide treatment.	RESULTS
+221	228	mutants	protein_state	To assess the effects of MKP7 and its mutants on the activation of endogenous JNK in vivo, HEK293T cells were transfected with blank vector or with HA-tagged constructs for full-length MKP7, MKP7ΔC304 and MKP7-CD or MKP7 mutants, and stimulated with ultraviolet or etoposide treatment.	RESULTS
+265	274	etoposide	chemical	To assess the effects of MKP7 and its mutants on the activation of endogenous JNK in vivo, HEK293T cells were transfected with blank vector or with HA-tagged constructs for full-length MKP7, MKP7ΔC304 and MKP7-CD or MKP7 mutants, and stimulated with ultraviolet or etoposide treatment.	RESULTS
+23	36	immunobloting	experimental_method	As shown in Fig. 6a–c, immunobloting showed similar expression levels for the different MKP7 constructs in all the cells.	RESULTS
+88	92	MKP7	protein	As shown in Fig. 6a–c, immunobloting showed similar expression levels for the different MKP7 constructs in all the cells.	RESULTS
+0	13	Overexpressed	experimental_method	Overexpressed full-length MKP7, MKP7ΔC304 and MKP7-CD significantly reduced the endogenous level of phosphorylated JNK compared with vector-transfected cells.	RESULTS
+14	25	full-length	protein_state	Overexpressed full-length MKP7, MKP7ΔC304 and MKP7-CD significantly reduced the endogenous level of phosphorylated JNK compared with vector-transfected cells.	RESULTS
+26	30	MKP7	protein	Overexpressed full-length MKP7, MKP7ΔC304 and MKP7-CD significantly reduced the endogenous level of phosphorylated JNK compared with vector-transfected cells.	RESULTS
+32	41	MKP7ΔC304	mutant	Overexpressed full-length MKP7, MKP7ΔC304 and MKP7-CD significantly reduced the endogenous level of phosphorylated JNK compared with vector-transfected cells.	RESULTS
+46	50	MKP7	protein	Overexpressed full-length MKP7, MKP7ΔC304 and MKP7-CD significantly reduced the endogenous level of phosphorylated JNK compared with vector-transfected cells.	RESULTS
+51	53	CD	structure_element	Overexpressed full-length MKP7, MKP7ΔC304 and MKP7-CD significantly reduced the endogenous level of phosphorylated JNK compared with vector-transfected cells.	RESULTS
+100	114	phosphorylated	protein_state	Overexpressed full-length MKP7, MKP7ΔC304 and MKP7-CD significantly reduced the endogenous level of phosphorylated JNK compared with vector-transfected cells.	RESULTS
+115	118	JNK	protein_type	Overexpressed full-length MKP7, MKP7ΔC304 and MKP7-CD significantly reduced the endogenous level of phosphorylated JNK compared with vector-transfected cells.	RESULTS
+45	52	D-motif	structure_element	Parallel experiments showed clearly that the D-motif mutants (R56A/R57A and V63A/I65A) dephosphorylated JNK as did the wild type under the same conditions, further confirming that the MKP7-KBD is not required for the JNK inactivation in vivo.	RESULTS
+53	60	mutants	protein_state	Parallel experiments showed clearly that the D-motif mutants (R56A/R57A and V63A/I65A) dephosphorylated JNK as did the wild type under the same conditions, further confirming that the MKP7-KBD is not required for the JNK inactivation in vivo.	RESULTS
+62	66	R56A	mutant	Parallel experiments showed clearly that the D-motif mutants (R56A/R57A and V63A/I65A) dephosphorylated JNK as did the wild type under the same conditions, further confirming that the MKP7-KBD is not required for the JNK inactivation in vivo.	RESULTS
+67	71	R57A	mutant	Parallel experiments showed clearly that the D-motif mutants (R56A/R57A and V63A/I65A) dephosphorylated JNK as did the wild type under the same conditions, further confirming that the MKP7-KBD is not required for the JNK inactivation in vivo.	RESULTS
+76	80	V63A	mutant	Parallel experiments showed clearly that the D-motif mutants (R56A/R57A and V63A/I65A) dephosphorylated JNK as did the wild type under the same conditions, further confirming that the MKP7-KBD is not required for the JNK inactivation in vivo.	RESULTS
+81	85	I65A	mutant	Parallel experiments showed clearly that the D-motif mutants (R56A/R57A and V63A/I65A) dephosphorylated JNK as did the wild type under the same conditions, further confirming that the MKP7-KBD is not required for the JNK inactivation in vivo.	RESULTS
+87	103	dephosphorylated	protein_state	Parallel experiments showed clearly that the D-motif mutants (R56A/R57A and V63A/I65A) dephosphorylated JNK as did the wild type under the same conditions, further confirming that the MKP7-KBD is not required for the JNK inactivation in vivo.	RESULTS
+104	107	JNK	protein_type	Parallel experiments showed clearly that the D-motif mutants (R56A/R57A and V63A/I65A) dephosphorylated JNK as did the wild type under the same conditions, further confirming that the MKP7-KBD is not required for the JNK inactivation in vivo.	RESULTS
+119	128	wild type	protein_state	Parallel experiments showed clearly that the D-motif mutants (R56A/R57A and V63A/I65A) dephosphorylated JNK as did the wild type under the same conditions, further confirming that the MKP7-KBD is not required for the JNK inactivation in vivo.	RESULTS
+184	188	MKP7	protein	Parallel experiments showed clearly that the D-motif mutants (R56A/R57A and V63A/I65A) dephosphorylated JNK as did the wild type under the same conditions, further confirming that the MKP7-KBD is not required for the JNK inactivation in vivo.	RESULTS
+189	192	KBD	structure_element	Parallel experiments showed clearly that the D-motif mutants (R56A/R57A and V63A/I65A) dephosphorylated JNK as did the wild type under the same conditions, further confirming that the MKP7-KBD is not required for the JNK inactivation in vivo.	RESULTS
+217	220	JNK	protein_type	Parallel experiments showed clearly that the D-motif mutants (R56A/R57A and V63A/I65A) dephosphorylated JNK as did the wild type under the same conditions, further confirming that the MKP7-KBD is not required for the JNK inactivation in vivo.	RESULTS
+48	62	phosphorylated	protein_state	Consistent with the in vitro data, the level of phosphorylated JNK was not or little altered in MKP7 FXF-motif mutants (F285D, F287D and L288D)-transfected cells, and the MKP7 D268A and N286A mutants retained the ability to reduce the phosphorylation levels of JNK.	RESULTS
+63	66	JNK	protein_type	Consistent with the in vitro data, the level of phosphorylated JNK was not or little altered in MKP7 FXF-motif mutants (F285D, F287D and L288D)-transfected cells, and the MKP7 D268A and N286A mutants retained the ability to reduce the phosphorylation levels of JNK.	RESULTS
+96	100	MKP7	protein	Consistent with the in vitro data, the level of phosphorylated JNK was not or little altered in MKP7 FXF-motif mutants (F285D, F287D and L288D)-transfected cells, and the MKP7 D268A and N286A mutants retained the ability to reduce the phosphorylation levels of JNK.	RESULTS
+101	110	FXF-motif	structure_element	Consistent with the in vitro data, the level of phosphorylated JNK was not or little altered in MKP7 FXF-motif mutants (F285D, F287D and L288D)-transfected cells, and the MKP7 D268A and N286A mutants retained the ability to reduce the phosphorylation levels of JNK.	RESULTS
+111	118	mutants	protein_state	Consistent with the in vitro data, the level of phosphorylated JNK was not or little altered in MKP7 FXF-motif mutants (F285D, F287D and L288D)-transfected cells, and the MKP7 D268A and N286A mutants retained the ability to reduce the phosphorylation levels of JNK.	RESULTS
+120	125	F285D	mutant	Consistent with the in vitro data, the level of phosphorylated JNK was not or little altered in MKP7 FXF-motif mutants (F285D, F287D and L288D)-transfected cells, and the MKP7 D268A and N286A mutants retained the ability to reduce the phosphorylation levels of JNK.	RESULTS
+127	132	F287D	mutant	Consistent with the in vitro data, the level of phosphorylated JNK was not or little altered in MKP7 FXF-motif mutants (F285D, F287D and L288D)-transfected cells, and the MKP7 D268A and N286A mutants retained the ability to reduce the phosphorylation levels of JNK.	RESULTS
+137	142	L288D	mutant	Consistent with the in vitro data, the level of phosphorylated JNK was not or little altered in MKP7 FXF-motif mutants (F285D, F287D and L288D)-transfected cells, and the MKP7 D268A and N286A mutants retained the ability to reduce the phosphorylation levels of JNK.	RESULTS
+171	175	MKP7	protein	Consistent with the in vitro data, the level of phosphorylated JNK was not or little altered in MKP7 FXF-motif mutants (F285D, F287D and L288D)-transfected cells, and the MKP7 D268A and N286A mutants retained the ability to reduce the phosphorylation levels of JNK.	RESULTS
+176	181	D268A	mutant	Consistent with the in vitro data, the level of phosphorylated JNK was not or little altered in MKP7 FXF-motif mutants (F285D, F287D and L288D)-transfected cells, and the MKP7 D268A and N286A mutants retained the ability to reduce the phosphorylation levels of JNK.	RESULTS
+186	191	N286A	mutant	Consistent with the in vitro data, the level of phosphorylated JNK was not or little altered in MKP7 FXF-motif mutants (F285D, F287D and L288D)-transfected cells, and the MKP7 D268A and N286A mutants retained the ability to reduce the phosphorylation levels of JNK.	RESULTS
+192	199	mutants	protein_state	Consistent with the in vitro data, the level of phosphorylated JNK was not or little altered in MKP7 FXF-motif mutants (F285D, F287D and L288D)-transfected cells, and the MKP7 D268A and N286A mutants retained the ability to reduce the phosphorylation levels of JNK.	RESULTS
+261	264	JNK	protein_type	Consistent with the in vitro data, the level of phosphorylated JNK was not or little altered in MKP7 FXF-motif mutants (F285D, F287D and L288D)-transfected cells, and the MKP7 D268A and N286A mutants retained the ability to reduce the phosphorylation levels of JNK.	RESULTS
+44	48	JNK1	protein	We next tested in vivo interactions between JNK1 mutants and full-length MKP7 by coimmunoprecipitation experiments under unstimulated conditions.	RESULTS
+49	56	mutants	protein_state	We next tested in vivo interactions between JNK1 mutants and full-length MKP7 by coimmunoprecipitation experiments under unstimulated conditions.	RESULTS
+61	72	full-length	protein_state	We next tested in vivo interactions between JNK1 mutants and full-length MKP7 by coimmunoprecipitation experiments under unstimulated conditions.	RESULTS
+73	77	MKP7	protein	We next tested in vivo interactions between JNK1 mutants and full-length MKP7 by coimmunoprecipitation experiments under unstimulated conditions.	RESULTS
+81	114	coimmunoprecipitation experiments	experimental_method	We next tested in vivo interactions between JNK1 mutants and full-length MKP7 by coimmunoprecipitation experiments under unstimulated conditions.	RESULTS
+5	17	co-expressed	experimental_method	When co-expressed in HEK293T cells, wild-type (HA)-JNK1 was readily precipitated with (Myc)-MKP7 (Fig. 6d), indicating that MKP7 binds dephosphorylated JNK1 protein in vivo.	RESULTS
+36	45	wild-type	protein_state	When co-expressed in HEK293T cells, wild-type (HA)-JNK1 was readily precipitated with (Myc)-MKP7 (Fig. 6d), indicating that MKP7 binds dephosphorylated JNK1 protein in vivo.	RESULTS
+51	55	JNK1	protein	When co-expressed in HEK293T cells, wild-type (HA)-JNK1 was readily precipitated with (Myc)-MKP7 (Fig. 6d), indicating that MKP7 binds dephosphorylated JNK1 protein in vivo.	RESULTS
+92	96	MKP7	protein	When co-expressed in HEK293T cells, wild-type (HA)-JNK1 was readily precipitated with (Myc)-MKP7 (Fig. 6d), indicating that MKP7 binds dephosphorylated JNK1 protein in vivo.	RESULTS
+124	128	MKP7	protein	When co-expressed in HEK293T cells, wild-type (HA)-JNK1 was readily precipitated with (Myc)-MKP7 (Fig. 6d), indicating that MKP7 binds dephosphorylated JNK1 protein in vivo.	RESULTS
+135	151	dephosphorylated	protein_state	When co-expressed in HEK293T cells, wild-type (HA)-JNK1 was readily precipitated with (Myc)-MKP7 (Fig. 6d), indicating that MKP7 binds dephosphorylated JNK1 protein in vivo.	RESULTS
+152	156	JNK1	protein	When co-expressed in HEK293T cells, wild-type (HA)-JNK1 was readily precipitated with (Myc)-MKP7 (Fig. 6d), indicating that MKP7 binds dephosphorylated JNK1 protein in vivo.	RESULTS
+22	40	in vitro pull-down	experimental_method	In agreement with the in vitro pull-down results, the mutants D229A, W234D and Y259D were not co-precipitated with MKP7, and the I231D mutant had only little effect on the JNK1–MKP7 interaction (Fig. 6d and Supplementary Fig. 3a).	RESULTS
+54	61	mutants	protein_state	In agreement with the in vitro pull-down results, the mutants D229A, W234D and Y259D were not co-precipitated with MKP7, and the I231D mutant had only little effect on the JNK1–MKP7 interaction (Fig. 6d and Supplementary Fig. 3a).	RESULTS
+62	67	D229A	mutant	In agreement with the in vitro pull-down results, the mutants D229A, W234D and Y259D were not co-precipitated with MKP7, and the I231D mutant had only little effect on the JNK1–MKP7 interaction (Fig. 6d and Supplementary Fig. 3a).	RESULTS
+69	74	W234D	mutant	In agreement with the in vitro pull-down results, the mutants D229A, W234D and Y259D were not co-precipitated with MKP7, and the I231D mutant had only little effect on the JNK1–MKP7 interaction (Fig. 6d and Supplementary Fig. 3a).	RESULTS
+79	84	Y259D	mutant	In agreement with the in vitro pull-down results, the mutants D229A, W234D and Y259D were not co-precipitated with MKP7, and the I231D mutant had only little effect on the JNK1–MKP7 interaction (Fig. 6d and Supplementary Fig. 3a).	RESULTS
+115	119	MKP7	protein	In agreement with the in vitro pull-down results, the mutants D229A, W234D and Y259D were not co-precipitated with MKP7, and the I231D mutant had only little effect on the JNK1–MKP7 interaction (Fig. 6d and Supplementary Fig. 3a).	RESULTS
+129	134	I231D	mutant	In agreement with the in vitro pull-down results, the mutants D229A, W234D and Y259D were not co-precipitated with MKP7, and the I231D mutant had only little effect on the JNK1–MKP7 interaction (Fig. 6d and Supplementary Fig. 3a).	RESULTS
+135	141	mutant	protein_state	In agreement with the in vitro pull-down results, the mutants D229A, W234D and Y259D were not co-precipitated with MKP7, and the I231D mutant had only little effect on the JNK1–MKP7 interaction (Fig. 6d and Supplementary Fig. 3a).	RESULTS
+172	181	JNK1–MKP7	complex_assembly	In agreement with the in vitro pull-down results, the mutants D229A, W234D and Y259D were not co-precipitated with MKP7, and the I231D mutant had only little effect on the JNK1–MKP7 interaction (Fig. 6d and Supplementary Fig. 3a).	RESULTS
+18	21	JNK	protein_type	Activation of the JNK signalling pathway is frequently associated with apoptotic cell death, and inhibition of JNK can prevent apoptotic death of multiple cells.	RESULTS
+111	114	JNK	protein_type	Activation of the JNK signalling pathway is frequently associated with apoptotic cell death, and inhibition of JNK can prevent apoptotic death of multiple cells.	RESULTS
+37	40	JNK	protein_type	To examine whether the inhibition of JNK activity by MKP7 would provide protections against the apoptosis, we analysed the rate of apoptosis in ultraviolet-irradiated cells transfected with MKP7 (wild type or mutants) by flow cytometry.	RESULTS
+53	57	MKP7	protein	To examine whether the inhibition of JNK activity by MKP7 would provide protections against the apoptosis, we analysed the rate of apoptosis in ultraviolet-irradiated cells transfected with MKP7 (wild type or mutants) by flow cytometry.	RESULTS
+190	194	MKP7	protein	To examine whether the inhibition of JNK activity by MKP7 would provide protections against the apoptosis, we analysed the rate of apoptosis in ultraviolet-irradiated cells transfected with MKP7 (wild type or mutants) by flow cytometry.	RESULTS
+196	205	wild type	protein_state	To examine whether the inhibition of JNK activity by MKP7 would provide protections against the apoptosis, we analysed the rate of apoptosis in ultraviolet-irradiated cells transfected with MKP7 (wild type or mutants) by flow cytometry.	RESULTS
+209	216	mutants	protein_state	To examine whether the inhibition of JNK activity by MKP7 would provide protections against the apoptosis, we analysed the rate of apoptosis in ultraviolet-irradiated cells transfected with MKP7 (wild type or mutants) by flow cytometry.	RESULTS
+221	235	flow cytometry	experimental_method	To examine whether the inhibition of JNK activity by MKP7 would provide protections against the apoptosis, we analysed the rate of apoptosis in ultraviolet-irradiated cells transfected with MKP7 (wild type or mutants) by flow cytometry.	RESULTS
+95	99	MKP7	protein	The results showed similar apoptotic rates between cells transfected with blank vector or with MKP7 (wild type or mutants) under unstimulated conditions (Supplementary Fig. 3b), while ultraviolet-irradiation significantly increased apoptotic rate in cells transfected with blank vector (Fig. 6e).	RESULTS
+101	110	wild type	protein_state	The results showed similar apoptotic rates between cells transfected with blank vector or with MKP7 (wild type or mutants) under unstimulated conditions (Supplementary Fig. 3b), while ultraviolet-irradiation significantly increased apoptotic rate in cells transfected with blank vector (Fig. 6e).	RESULTS
+114	121	mutants	protein_state	The results showed similar apoptotic rates between cells transfected with blank vector or with MKP7 (wild type or mutants) under unstimulated conditions (Supplementary Fig. 3b), while ultraviolet-irradiation significantly increased apoptotic rate in cells transfected with blank vector (Fig. 6e).	RESULTS
+0	11	Expressions	experimental_method	Expressions of wild-type MKP7, MKP7ΔC304 and MKP7-CD significantly decreased the proportion of apoptotic cells after ultraviolet treatment.	RESULTS
+15	24	wild-type	protein_state	Expressions of wild-type MKP7, MKP7ΔC304 and MKP7-CD significantly decreased the proportion of apoptotic cells after ultraviolet treatment.	RESULTS
+25	29	MKP7	protein	Expressions of wild-type MKP7, MKP7ΔC304 and MKP7-CD significantly decreased the proportion of apoptotic cells after ultraviolet treatment.	RESULTS
+31	40	MKP7ΔC304	mutant	Expressions of wild-type MKP7, MKP7ΔC304 and MKP7-CD significantly decreased the proportion of apoptotic cells after ultraviolet treatment.	RESULTS
+45	49	MKP7	protein	Expressions of wild-type MKP7, MKP7ΔC304 and MKP7-CD significantly decreased the proportion of apoptotic cells after ultraviolet treatment.	RESULTS
+50	52	CD	structure_element	Expressions of wild-type MKP7, MKP7ΔC304 and MKP7-CD significantly decreased the proportion of apoptotic cells after ultraviolet treatment.	RESULTS
+40	44	MKP7	protein	Moreover, treatment of cells expressing MKP7-KBD mutants (R56A/R57A and V63A/I65A) decreased the apoptosis rates to a similar extent as MKP7 wild type did.	RESULTS
+45	48	KBD	structure_element	Moreover, treatment of cells expressing MKP7-KBD mutants (R56A/R57A and V63A/I65A) decreased the apoptosis rates to a similar extent as MKP7 wild type did.	RESULTS
+49	56	mutants	protein_state	Moreover, treatment of cells expressing MKP7-KBD mutants (R56A/R57A and V63A/I65A) decreased the apoptosis rates to a similar extent as MKP7 wild type did.	RESULTS
+58	62	R56A	mutant	Moreover, treatment of cells expressing MKP7-KBD mutants (R56A/R57A and V63A/I65A) decreased the apoptosis rates to a similar extent as MKP7 wild type did.	RESULTS
+63	67	R57A	mutant	Moreover, treatment of cells expressing MKP7-KBD mutants (R56A/R57A and V63A/I65A) decreased the apoptosis rates to a similar extent as MKP7 wild type did.	RESULTS
+72	76	V63A	mutant	Moreover, treatment of cells expressing MKP7-KBD mutants (R56A/R57A and V63A/I65A) decreased the apoptosis rates to a similar extent as MKP7 wild type did.	RESULTS
+77	81	I65A	mutant	Moreover, treatment of cells expressing MKP7-KBD mutants (R56A/R57A and V63A/I65A) decreased the apoptosis rates to a similar extent as MKP7 wild type did.	RESULTS
+136	140	MKP7	protein	Moreover, treatment of cells expressing MKP7-KBD mutants (R56A/R57A and V63A/I65A) decreased the apoptosis rates to a similar extent as MKP7 wild type did.	RESULTS
+141	150	wild type	protein_state	Moreover, treatment of cells expressing MKP7-KBD mutants (R56A/R57A and V63A/I65A) decreased the apoptosis rates to a similar extent as MKP7 wild type did.	RESULTS
+40	44	MKP7	protein	In contrast, cells transfected with the MKP7 FXF-motif mutants (F285D, F287D and L288D) showed little protective effect after ultraviolet treatment and similar levels of apoptosis rates were detected to cells transfected with control vectors (Fig. 6e,f).	RESULTS
+45	54	FXF-motif	structure_element	In contrast, cells transfected with the MKP7 FXF-motif mutants (F285D, F287D and L288D) showed little protective effect after ultraviolet treatment and similar levels of apoptosis rates were detected to cells transfected with control vectors (Fig. 6e,f).	RESULTS
+55	62	mutants	protein_state	In contrast, cells transfected with the MKP7 FXF-motif mutants (F285D, F287D and L288D) showed little protective effect after ultraviolet treatment and similar levels of apoptosis rates were detected to cells transfected with control vectors (Fig. 6e,f).	RESULTS
+64	69	F285D	mutant	In contrast, cells transfected with the MKP7 FXF-motif mutants (F285D, F287D and L288D) showed little protective effect after ultraviolet treatment and similar levels of apoptosis rates were detected to cells transfected with control vectors (Fig. 6e,f).	RESULTS
+71	76	F287D	mutant	In contrast, cells transfected with the MKP7 FXF-motif mutants (F285D, F287D and L288D) showed little protective effect after ultraviolet treatment and similar levels of apoptosis rates were detected to cells transfected with control vectors (Fig. 6e,f).	RESULTS
+81	86	L288D	mutant	In contrast, cells transfected with the MKP7 FXF-motif mutants (F285D, F287D and L288D) showed little protective effect after ultraviolet treatment and similar levels of apoptosis rates were detected to cells transfected with control vectors (Fig. 6e,f).	RESULTS
+43	52	FXF-motif	structure_element	Taken together, our results suggested that FXF-motif-mediated, rather than KBD-mediated, interaction is essential for MKP7 to block ultraviolet-induced apoptosis.	RESULTS
+75	78	KBD	structure_element	Taken together, our results suggested that FXF-motif-mediated, rather than KBD-mediated, interaction is essential for MKP7 to block ultraviolet-induced apoptosis.	RESULTS
+118	122	MKP7	protein	Taken together, our results suggested that FXF-motif-mediated, rather than KBD-mediated, interaction is essential for MKP7 to block ultraviolet-induced apoptosis.	RESULTS
+32	36	JNK1	protein	A similar docking mechanism for JNK1 recognition by MKP5	RESULTS
+52	56	MKP5	protein	A similar docking mechanism for JNK1 recognition by MKP5	RESULTS
+0	4	MKP5	protein	MKP5 belongs to the same subfamily as MKP7.	RESULTS
+38	42	MKP7	protein	MKP5 belongs to the same subfamily as MKP7.	RESULTS
+0	4	MKP5	protein	MKP5 is unique among the MKPs in possessing an additional domain of unknown function at the N-terminus (Fig. 7a).	RESULTS
+25	29	MKPs	protein_type	MKP5 is unique among the MKPs in possessing an additional domain of unknown function at the N-terminus (Fig. 7a).	RESULTS
+4	7	KBD	structure_element	The KBD of MKP5 interacts with the D-site of p38α to mediate the enzyme–substrate interaction.	RESULTS
+11	15	MKP5	protein	The KBD of MKP5 interacts with the D-site of p38α to mediate the enzyme–substrate interaction.	RESULTS
+35	41	D-site	site	The KBD of MKP5 interacts with the D-site of p38α to mediate the enzyme–substrate interaction.	RESULTS
+45	49	p38α	protein	The KBD of MKP5 interacts with the D-site of p38α to mediate the enzyme–substrate interaction.	RESULTS
+0	11	Deletion of	experimental_method	Deletion of the KBD in MKP5 leads to a 280-fold increase in Km for p38α substrate.	RESULTS
+16	19	KBD	structure_element	Deletion of the KBD in MKP5 leads to a 280-fold increase in Km for p38α substrate.	RESULTS
+23	27	MKP5	protein	Deletion of the KBD in MKP5 leads to a 280-fold increase in Km for p38α substrate.	RESULTS
+60	62	Km	evidence	Deletion of the KBD in MKP5 leads to a 280-fold increase in Km for p38α substrate.	RESULTS
+67	71	p38α	protein	Deletion of the KBD in MKP5 leads to a 280-fold increase in Km for p38α substrate.	RESULTS
+15	19	p38α	protein	In contrast to p38α substrate, deletion of the MKP5-KBD had little effects on the kinetic parameters for the JNK1 dephosphorylation, indicating that the KBD of MKP5 is not required for the JNK1 dephosphorylation (Fig. 7b).	RESULTS
+31	42	deletion of	experimental_method	In contrast to p38α substrate, deletion of the MKP5-KBD had little effects on the kinetic parameters for the JNK1 dephosphorylation, indicating that the KBD of MKP5 is not required for the JNK1 dephosphorylation (Fig. 7b).	RESULTS
+47	51	MKP5	protein	In contrast to p38α substrate, deletion of the MKP5-KBD had little effects on the kinetic parameters for the JNK1 dephosphorylation, indicating that the KBD of MKP5 is not required for the JNK1 dephosphorylation (Fig. 7b).	RESULTS
+52	55	KBD	structure_element	In contrast to p38α substrate, deletion of the MKP5-KBD had little effects on the kinetic parameters for the JNK1 dephosphorylation, indicating that the KBD of MKP5 is not required for the JNK1 dephosphorylation (Fig. 7b).	RESULTS
+109	113	JNK1	protein	In contrast to p38α substrate, deletion of the MKP5-KBD had little effects on the kinetic parameters for the JNK1 dephosphorylation, indicating that the KBD of MKP5 is not required for the JNK1 dephosphorylation (Fig. 7b).	RESULTS
+153	156	KBD	structure_element	In contrast to p38α substrate, deletion of the MKP5-KBD had little effects on the kinetic parameters for the JNK1 dephosphorylation, indicating that the KBD of MKP5 is not required for the JNK1 dephosphorylation (Fig. 7b).	RESULTS
+160	164	MKP5	protein	In contrast to p38α substrate, deletion of the MKP5-KBD had little effects on the kinetic parameters for the JNK1 dephosphorylation, indicating that the KBD of MKP5 is not required for the JNK1 dephosphorylation (Fig. 7b).	RESULTS
+189	193	JNK1	protein	In contrast to p38α substrate, deletion of the MKP5-KBD had little effects on the kinetic parameters for the JNK1 dephosphorylation, indicating that the KBD of MKP5 is not required for the JNK1 dephosphorylation (Fig. 7b).	RESULTS
+4	34	substrate specificity constant	evidence	The substrate specificity constant kcat /Km value for MKP5-CD was calculated as 1.0 × 105 M−1 s−1, which is very close to that of MKP7-CD (1.07 × 105 M−1 s−1).	RESULTS
+35	43	kcat /Km	evidence	The substrate specificity constant kcat /Km value for MKP5-CD was calculated as 1.0 × 105 M−1 s−1, which is very close to that of MKP7-CD (1.07 × 105 M−1 s−1).	RESULTS
+54	58	MKP5	protein	The substrate specificity constant kcat /Km value for MKP5-CD was calculated as 1.0 × 105 M−1 s−1, which is very close to that of MKP7-CD (1.07 × 105 M−1 s−1).	RESULTS
+59	61	CD	structure_element	The substrate specificity constant kcat /Km value for MKP5-CD was calculated as 1.0 × 105 M−1 s−1, which is very close to that of MKP7-CD (1.07 × 105 M−1 s−1).	RESULTS
+130	134	MKP7	protein	The substrate specificity constant kcat /Km value for MKP5-CD was calculated as 1.0 × 105 M−1 s−1, which is very close to that of MKP7-CD (1.07 × 105 M−1 s−1).	RESULTS
+135	137	CD	structure_element	The substrate specificity constant kcat /Km value for MKP5-CD was calculated as 1.0 × 105 M−1 s−1, which is very close to that of MKP7-CD (1.07 × 105 M−1 s−1).	RESULTS
+4	21	crystal structure	evidence	The crystal structure of human MKP5-CD has been determined.	RESULTS
+25	30	human	species	The crystal structure of human MKP5-CD has been determined.	RESULTS
+31	35	MKP5	protein	The crystal structure of human MKP5-CD has been determined.	RESULTS
+36	38	CD	structure_element	The crystal structure of human MKP5-CD has been determined.	RESULTS
+20	37	catalytic domains	structure_element	Comparisons between catalytic domains structures of MKP5 and MKP7 reveal that the overall folds of the two proteins are highly similar, with only a few regions exhibiting small deviations (r.m.s.d. of 0.79 Å; Fig. 7c).	RESULTS
+38	48	structures	evidence	Comparisons between catalytic domains structures of MKP5 and MKP7 reveal that the overall folds of the two proteins are highly similar, with only a few regions exhibiting small deviations (r.m.s.d. of 0.79 Å; Fig. 7c).	RESULTS
+52	56	MKP5	protein	Comparisons between catalytic domains structures of MKP5 and MKP7 reveal that the overall folds of the two proteins are highly similar, with only a few regions exhibiting small deviations (r.m.s.d. of 0.79 Å; Fig. 7c).	RESULTS
+61	65	MKP7	protein	Comparisons between catalytic domains structures of MKP5 and MKP7 reveal that the overall folds of the two proteins are highly similar, with only a few regions exhibiting small deviations (r.m.s.d. of 0.79 Å; Fig. 7c).	RESULTS
+189	197	r.m.s.d.	evidence	Comparisons between catalytic domains structures of MKP5 and MKP7 reveal that the overall folds of the two proteins are highly similar, with only a few regions exhibiting small deviations (r.m.s.d. of 0.79 Å; Fig. 7c).	RESULTS
+52	69	crystal structure	evidence	Given the distinct interaction mode revealed by the crystal structure of JNK1–MKP7-CD, one obvious question is whether this is a general mechanism used by all members of the JNK-specific MKPs.	RESULTS
+73	85	JNK1–MKP7-CD	complex_assembly	Given the distinct interaction mode revealed by the crystal structure of JNK1–MKP7-CD, one obvious question is whether this is a general mechanism used by all members of the JNK-specific MKPs.	RESULTS
+174	191	JNK-specific MKPs	protein_type	Given the distinct interaction mode revealed by the crystal structure of JNK1–MKP7-CD, one obvious question is whether this is a general mechanism used by all members of the JNK-specific MKPs.	RESULTS
+64	68	JNK1	protein	To address this issue, we first examined the docking ability of JNK1 to the KBD and CD of MKP5 using gel filtration analysis and pull-down assays.	RESULTS
+76	79	KBD	structure_element	To address this issue, we first examined the docking ability of JNK1 to the KBD and CD of MKP5 using gel filtration analysis and pull-down assays.	RESULTS
+84	86	CD	structure_element	To address this issue, we first examined the docking ability of JNK1 to the KBD and CD of MKP5 using gel filtration analysis and pull-down assays.	RESULTS
+90	94	MKP5	protein	To address this issue, we first examined the docking ability of JNK1 to the KBD and CD of MKP5 using gel filtration analysis and pull-down assays.	RESULTS
+101	124	gel filtration analysis	experimental_method	To address this issue, we first examined the docking ability of JNK1 to the KBD and CD of MKP5 using gel filtration analysis and pull-down assays.	RESULTS
+129	145	pull-down assays	experimental_method	To address this issue, we first examined the docking ability of JNK1 to the KBD and CD of MKP5 using gel filtration analysis and pull-down assays.	RESULTS
+20	46	gel filtration experiments	experimental_method	It can be seen from gel filtration experiments that JNK1 can forms a stable heterodimer with MKP5-CD in solution, but no detectable interaction was found with the KBD domain (Fig. 7d).	RESULTS
+52	56	JNK1	protein	It can be seen from gel filtration experiments that JNK1 can forms a stable heterodimer with MKP5-CD in solution, but no detectable interaction was found with the KBD domain (Fig. 7d).	RESULTS
+69	75	stable	protein_state	It can be seen from gel filtration experiments that JNK1 can forms a stable heterodimer with MKP5-CD in solution, but no detectable interaction was found with the KBD domain (Fig. 7d).	RESULTS
+76	87	heterodimer	oligomeric_state	It can be seen from gel filtration experiments that JNK1 can forms a stable heterodimer with MKP5-CD in solution, but no detectable interaction was found with the KBD domain (Fig. 7d).	RESULTS
+93	97	MKP5	protein	It can be seen from gel filtration experiments that JNK1 can forms a stable heterodimer with MKP5-CD in solution, but no detectable interaction was found with the KBD domain (Fig. 7d).	RESULTS
+98	100	CD	structure_element	It can be seen from gel filtration experiments that JNK1 can forms a stable heterodimer with MKP5-CD in solution, but no detectable interaction was found with the KBD domain (Fig. 7d).	RESULTS
+163	166	KBD	structure_element	It can be seen from gel filtration experiments that JNK1 can forms a stable heterodimer with MKP5-CD in solution, but no detectable interaction was found with the KBD domain (Fig. 7d).	RESULTS
+0	16	Pull-down assays	experimental_method	Pull-down assays also confirmed the protein–protein interactions observed above.	RESULTS
+4	20	catalytic domain	structure_element	The catalytic domain of MKP5, but not its KBD, was able to pull-down a detectable amount of JNK1 (Fig. 7e), implicating a different substrate-recognition mechanisms for p38 and JNK MAPKs.	RESULTS
+24	28	MKP5	protein	The catalytic domain of MKP5, but not its KBD, was able to pull-down a detectable amount of JNK1 (Fig. 7e), implicating a different substrate-recognition mechanisms for p38 and JNK MAPKs.	RESULTS
+42	45	KBD	structure_element	The catalytic domain of MKP5, but not its KBD, was able to pull-down a detectable amount of JNK1 (Fig. 7e), implicating a different substrate-recognition mechanisms for p38 and JNK MAPKs.	RESULTS
+92	96	JNK1	protein	The catalytic domain of MKP5, but not its KBD, was able to pull-down a detectable amount of JNK1 (Fig. 7e), implicating a different substrate-recognition mechanisms for p38 and JNK MAPKs.	RESULTS
+169	172	p38	protein_type	The catalytic domain of MKP5, but not its KBD, was able to pull-down a detectable amount of JNK1 (Fig. 7e), implicating a different substrate-recognition mechanisms for p38 and JNK MAPKs.	RESULTS
+177	180	JNK	protein_type	The catalytic domain of MKP5, but not its KBD, was able to pull-down a detectable amount of JNK1 (Fig. 7e), implicating a different substrate-recognition mechanisms for p38 and JNK MAPKs.	RESULTS
+181	186	MAPKs	protein_type	The catalytic domain of MKP5, but not its KBD, was able to pull-down a detectable amount of JNK1 (Fig. 7e), implicating a different substrate-recognition mechanisms for p38 and JNK MAPKs.	RESULTS
+54	58	MKP5	protein	To further test our hypothesis, we generated forms of MKP5-CD bearing mutations corresponding to the changes we made on MKP7-CD on the basis of sequence and structural alignment and examined their effects on the phosphatase activity.	RESULTS
+59	61	CD	structure_element	To further test our hypothesis, we generated forms of MKP5-CD bearing mutations corresponding to the changes we made on MKP7-CD on the basis of sequence and structural alignment and examined their effects on the phosphatase activity.	RESULTS
+70	79	mutations	experimental_method	To further test our hypothesis, we generated forms of MKP5-CD bearing mutations corresponding to the changes we made on MKP7-CD on the basis of sequence and structural alignment and examined their effects on the phosphatase activity.	RESULTS
+120	124	MKP7	protein	To further test our hypothesis, we generated forms of MKP5-CD bearing mutations corresponding to the changes we made on MKP7-CD on the basis of sequence and structural alignment and examined their effects on the phosphatase activity.	RESULTS
+125	127	CD	structure_element	To further test our hypothesis, we generated forms of MKP5-CD bearing mutations corresponding to the changes we made on MKP7-CD on the basis of sequence and structural alignment and examined their effects on the phosphatase activity.	RESULTS
+144	177	sequence and structural alignment	experimental_method	To further test our hypothesis, we generated forms of MKP5-CD bearing mutations corresponding to the changes we made on MKP7-CD on the basis of sequence and structural alignment and examined their effects on the phosphatase activity.	RESULTS
+212	223	phosphatase	protein_type	To further test our hypothesis, we generated forms of MKP5-CD bearing mutations corresponding to the changes we made on MKP7-CD on the basis of sequence and structural alignment and examined their effects on the phosphatase activity.	RESULTS
+25	30	T432A	mutant	As shown in Fig. 7f, the T432A and L449F MKP5 mutant showed little or no difference in phosphatase activity, whereas the other mutants showed reduced specific activities of MKP5.	RESULTS
+35	40	L449F	mutant	As shown in Fig. 7f, the T432A and L449F MKP5 mutant showed little or no difference in phosphatase activity, whereas the other mutants showed reduced specific activities of MKP5.	RESULTS
+41	45	MKP5	protein	As shown in Fig. 7f, the T432A and L449F MKP5 mutant showed little or no difference in phosphatase activity, whereas the other mutants showed reduced specific activities of MKP5.	RESULTS
+46	52	mutant	protein_state	As shown in Fig. 7f, the T432A and L449F MKP5 mutant showed little or no difference in phosphatase activity, whereas the other mutants showed reduced specific activities of MKP5.	RESULTS
+127	134	mutants	protein_state	As shown in Fig. 7f, the T432A and L449F MKP5 mutant showed little or no difference in phosphatase activity, whereas the other mutants showed reduced specific activities of MKP5.	RESULTS
+173	177	MKP5	protein	As shown in Fig. 7f, the T432A and L449F MKP5 mutant showed little or no difference in phosphatase activity, whereas the other mutants showed reduced specific activities of MKP5.	RESULTS
+18	22	MKP7	protein	As in the case of MKP7, all the mutants, except F451D/A, showed no pNPPase activity changes compared with the wild-type MKP5-CD (Fig. 7g), and the point mutations in JNK1 also reduced the binding affinity of MKP5-CD for JNK1 (Fig. 7h).	RESULTS
+32	39	mutants	protein_state	As in the case of MKP7, all the mutants, except F451D/A, showed no pNPPase activity changes compared with the wild-type MKP5-CD (Fig. 7g), and the point mutations in JNK1 also reduced the binding affinity of MKP5-CD for JNK1 (Fig. 7h).	RESULTS
+48	55	F451D/A	mutant	As in the case of MKP7, all the mutants, except F451D/A, showed no pNPPase activity changes compared with the wild-type MKP5-CD (Fig. 7g), and the point mutations in JNK1 also reduced the binding affinity of MKP5-CD for JNK1 (Fig. 7h).	RESULTS
+67	74	pNPPase	protein_type	As in the case of MKP7, all the mutants, except F451D/A, showed no pNPPase activity changes compared with the wild-type MKP5-CD (Fig. 7g), and the point mutations in JNK1 also reduced the binding affinity of MKP5-CD for JNK1 (Fig. 7h).	RESULTS
+110	119	wild-type	protein_state	As in the case of MKP7, all the mutants, except F451D/A, showed no pNPPase activity changes compared with the wild-type MKP5-CD (Fig. 7g), and the point mutations in JNK1 also reduced the binding affinity of MKP5-CD for JNK1 (Fig. 7h).	RESULTS
+120	124	MKP5	protein	As in the case of MKP7, all the mutants, except F451D/A, showed no pNPPase activity changes compared with the wild-type MKP5-CD (Fig. 7g), and the point mutations in JNK1 also reduced the binding affinity of MKP5-CD for JNK1 (Fig. 7h).	RESULTS
+125	127	CD	structure_element	As in the case of MKP7, all the mutants, except F451D/A, showed no pNPPase activity changes compared with the wild-type MKP5-CD (Fig. 7g), and the point mutations in JNK1 also reduced the binding affinity of MKP5-CD for JNK1 (Fig. 7h).	RESULTS
+147	162	point mutations	experimental_method	As in the case of MKP7, all the mutants, except F451D/A, showed no pNPPase activity changes compared with the wild-type MKP5-CD (Fig. 7g), and the point mutations in JNK1 also reduced the binding affinity of MKP5-CD for JNK1 (Fig. 7h).	RESULTS
+166	170	JNK1	protein	As in the case of MKP7, all the mutants, except F451D/A, showed no pNPPase activity changes compared with the wild-type MKP5-CD (Fig. 7g), and the point mutations in JNK1 also reduced the binding affinity of MKP5-CD for JNK1 (Fig. 7h).	RESULTS
+188	204	binding affinity	evidence	As in the case of MKP7, all the mutants, except F451D/A, showed no pNPPase activity changes compared with the wild-type MKP5-CD (Fig. 7g), and the point mutations in JNK1 also reduced the binding affinity of MKP5-CD for JNK1 (Fig. 7h).	RESULTS
+208	212	MKP5	protein	As in the case of MKP7, all the mutants, except F451D/A, showed no pNPPase activity changes compared with the wild-type MKP5-CD (Fig. 7g), and the point mutations in JNK1 also reduced the binding affinity of MKP5-CD for JNK1 (Fig. 7h).	RESULTS
+213	215	CD	structure_element	As in the case of MKP7, all the mutants, except F451D/A, showed no pNPPase activity changes compared with the wild-type MKP5-CD (Fig. 7g), and the point mutations in JNK1 also reduced the binding affinity of MKP5-CD for JNK1 (Fig. 7h).	RESULTS
+220	224	JNK1	protein	As in the case of MKP7, all the mutants, except F451D/A, showed no pNPPase activity changes compared with the wild-type MKP5-CD (Fig. 7g), and the point mutations in JNK1 also reduced the binding affinity of MKP5-CD for JNK1 (Fig. 7h).	RESULTS
+58	68	CD spectra	evidence	In addition, there were no significant differences in the CD spectra between wild-type and mutant proteins, indicating that the overall structures of these mutants did not change significantly from that of wild-type MKP5 protein (Supplementary Fig. 4a).	RESULTS
+77	86	wild-type	protein_state	In addition, there were no significant differences in the CD spectra between wild-type and mutant proteins, indicating that the overall structures of these mutants did not change significantly from that of wild-type MKP5 protein (Supplementary Fig. 4a).	RESULTS
+91	97	mutant	protein_state	In addition, there were no significant differences in the CD spectra between wild-type and mutant proteins, indicating that the overall structures of these mutants did not change significantly from that of wild-type MKP5 protein (Supplementary Fig. 4a).	RESULTS
+136	146	structures	evidence	In addition, there were no significant differences in the CD spectra between wild-type and mutant proteins, indicating that the overall structures of these mutants did not change significantly from that of wild-type MKP5 protein (Supplementary Fig. 4a).	RESULTS
+156	163	mutants	protein_state	In addition, there were no significant differences in the CD spectra between wild-type and mutant proteins, indicating that the overall structures of these mutants did not change significantly from that of wild-type MKP5 protein (Supplementary Fig. 4a).	RESULTS
+206	215	wild-type	protein_state	In addition, there were no significant differences in the CD spectra between wild-type and mutant proteins, indicating that the overall structures of these mutants did not change significantly from that of wild-type MKP5 protein (Supplementary Fig. 4a).	RESULTS
+216	220	MKP5	protein	In addition, there were no significant differences in the CD spectra between wild-type and mutant proteins, indicating that the overall structures of these mutants did not change significantly from that of wild-type MKP5 protein (Supplementary Fig. 4a).	RESULTS
+41	45	MKP5	protein	Taken together, our results suggest that MKP5 binds JNK1 in a docking mode similar to that in the JNK1–MKP7 complex, and the detailed interaction model can be generated using molecular dynamics simulation based on the structure of JNK1–MKP7-CD complex (Supplementary Fig. 4b,c).	RESULTS
+52	56	JNK1	protein	Taken together, our results suggest that MKP5 binds JNK1 in a docking mode similar to that in the JNK1–MKP7 complex, and the detailed interaction model can be generated using molecular dynamics simulation based on the structure of JNK1–MKP7-CD complex (Supplementary Fig. 4b,c).	RESULTS
+98	107	JNK1–MKP7	complex_assembly	Taken together, our results suggest that MKP5 binds JNK1 in a docking mode similar to that in the JNK1–MKP7 complex, and the detailed interaction model can be generated using molecular dynamics simulation based on the structure of JNK1–MKP7-CD complex (Supplementary Fig. 4b,c).	RESULTS
+175	204	molecular dynamics simulation	experimental_method	Taken together, our results suggest that MKP5 binds JNK1 in a docking mode similar to that in the JNK1–MKP7 complex, and the detailed interaction model can be generated using molecular dynamics simulation based on the structure of JNK1–MKP7-CD complex (Supplementary Fig. 4b,c).	RESULTS
+218	227	structure	evidence	Taken together, our results suggest that MKP5 binds JNK1 in a docking mode similar to that in the JNK1–MKP7 complex, and the detailed interaction model can be generated using molecular dynamics simulation based on the structure of JNK1–MKP7-CD complex (Supplementary Fig. 4b,c).	RESULTS
+231	243	JNK1–MKP7-CD	complex_assembly	Taken together, our results suggest that MKP5 binds JNK1 in a docking mode similar to that in the JNK1–MKP7 complex, and the detailed interaction model can be generated using molecular dynamics simulation based on the structure of JNK1–MKP7-CD complex (Supplementary Fig. 4b,c).	RESULTS
+19	23	MKP5	protein	In this model, the MKP5-CD adopts a conformation nearly identical to that in its unbound form, suggesting that the conformation of the catalytic domain undergoes little change, if any at all, upon JNK1 binding.	RESULTS
+24	26	CD	structure_element	In this model, the MKP5-CD adopts a conformation nearly identical to that in its unbound form, suggesting that the conformation of the catalytic domain undergoes little change, if any at all, upon JNK1 binding.	RESULTS
+81	88	unbound	protein_state	In this model, the MKP5-CD adopts a conformation nearly identical to that in its unbound form, suggesting that the conformation of the catalytic domain undergoes little change, if any at all, upon JNK1 binding.	RESULTS
+135	151	catalytic domain	structure_element	In this model, the MKP5-CD adopts a conformation nearly identical to that in its unbound form, suggesting that the conformation of the catalytic domain undergoes little change, if any at all, upon JNK1 binding.	RESULTS
+197	201	JNK1	protein	In this model, the MKP5-CD adopts a conformation nearly identical to that in its unbound form, suggesting that the conformation of the catalytic domain undergoes little change, if any at all, upon JNK1 binding.	RESULTS
+15	21	Leu449	residue_name_number	In particular, Leu449 of MKP5, which is equivalent to the key residue Phe285 of MKP7, buried deeply within the hydrophobic pocket of JNK1 in the same way as Phe285 in the JNK1–MKP7-CD complex (Supplementary Fig. 4d).	RESULTS
+25	29	MKP5	protein	In particular, Leu449 of MKP5, which is equivalent to the key residue Phe285 of MKP7, buried deeply within the hydrophobic pocket of JNK1 in the same way as Phe285 in the JNK1–MKP7-CD complex (Supplementary Fig. 4d).	RESULTS
+70	76	Phe285	residue_name_number	In particular, Leu449 of MKP5, which is equivalent to the key residue Phe285 of MKP7, buried deeply within the hydrophobic pocket of JNK1 in the same way as Phe285 in the JNK1–MKP7-CD complex (Supplementary Fig. 4d).	RESULTS
+80	84	MKP7	protein	In particular, Leu449 of MKP5, which is equivalent to the key residue Phe285 of MKP7, buried deeply within the hydrophobic pocket of JNK1 in the same way as Phe285 in the JNK1–MKP7-CD complex (Supplementary Fig. 4d).	RESULTS
+111	129	hydrophobic pocket	site	In particular, Leu449 of MKP5, which is equivalent to the key residue Phe285 of MKP7, buried deeply within the hydrophobic pocket of JNK1 in the same way as Phe285 in the JNK1–MKP7-CD complex (Supplementary Fig. 4d).	RESULTS
+133	137	JNK1	protein	In particular, Leu449 of MKP5, which is equivalent to the key residue Phe285 of MKP7, buried deeply within the hydrophobic pocket of JNK1 in the same way as Phe285 in the JNK1–MKP7-CD complex (Supplementary Fig. 4d).	RESULTS
+157	163	Phe285	residue_name_number	In particular, Leu449 of MKP5, which is equivalent to the key residue Phe285 of MKP7, buried deeply within the hydrophobic pocket of JNK1 in the same way as Phe285 in the JNK1–MKP7-CD complex (Supplementary Fig. 4d).	RESULTS
+171	183	JNK1–MKP7-CD	complex_assembly	In particular, Leu449 of MKP5, which is equivalent to the key residue Phe285 of MKP7, buried deeply within the hydrophobic pocket of JNK1 in the same way as Phe285 in the JNK1–MKP7-CD complex (Supplementary Fig. 4d).	RESULTS
+40	44	JNK1	protein	Despite the strong similarities between JNK1–MKP5-CD and JNK1–MKP7-CD, however, there are differences.	RESULTS
+45	49	MKP5	protein	Despite the strong similarities between JNK1–MKP5-CD and JNK1–MKP7-CD, however, there are differences.	RESULTS
+50	52	CD	structure_element	Despite the strong similarities between JNK1–MKP5-CD and JNK1–MKP7-CD, however, there are differences.	RESULTS
+57	69	JNK1–MKP7-CD	complex_assembly	Despite the strong similarities between JNK1–MKP5-CD and JNK1–MKP7-CD, however, there are differences.	RESULTS
+4	16	JNK1–MKP7-CD	complex_assembly	The JNK1–MKP7-CD interaction is better and more extensive.	RESULTS
+0	6	Asp268	residue_name_number	Asp268 of MKP7-CD forms salt bridge with JNK1 Arg263, whereas the corresponding residue Thr432 in MKP5-CD may not interact with JNK1.	RESULTS
+10	14	MKP7	protein	Asp268 of MKP7-CD forms salt bridge with JNK1 Arg263, whereas the corresponding residue Thr432 in MKP5-CD may not interact with JNK1.	RESULTS
+15	17	CD	structure_element	Asp268 of MKP7-CD forms salt bridge with JNK1 Arg263, whereas the corresponding residue Thr432 in MKP5-CD may not interact with JNK1.	RESULTS
+24	35	salt bridge	bond_interaction	Asp268 of MKP7-CD forms salt bridge with JNK1 Arg263, whereas the corresponding residue Thr432 in MKP5-CD may not interact with JNK1.	RESULTS
+41	45	JNK1	protein	Asp268 of MKP7-CD forms salt bridge with JNK1 Arg263, whereas the corresponding residue Thr432 in MKP5-CD may not interact with JNK1.	RESULTS
+46	52	Arg263	residue_name_number	Asp268 of MKP7-CD forms salt bridge with JNK1 Arg263, whereas the corresponding residue Thr432 in MKP5-CD may not interact with JNK1.	RESULTS
+88	94	Thr432	residue_name_number	Asp268 of MKP7-CD forms salt bridge with JNK1 Arg263, whereas the corresponding residue Thr432 in MKP5-CD may not interact with JNK1.	RESULTS
+98	102	MKP5	protein	Asp268 of MKP7-CD forms salt bridge with JNK1 Arg263, whereas the corresponding residue Thr432 in MKP5-CD may not interact with JNK1.	RESULTS
+103	105	CD	structure_element	Asp268 of MKP7-CD forms salt bridge with JNK1 Arg263, whereas the corresponding residue Thr432 in MKP5-CD may not interact with JNK1.	RESULTS
+128	132	JNK1	protein	Asp268 of MKP7-CD forms salt bridge with JNK1 Arg263, whereas the corresponding residue Thr432 in MKP5-CD may not interact with JNK1.	RESULTS
+45	49	MKP7	protein	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+50	52	CD	structure_element	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+54	60	Phe215	residue_name_number	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+62	68	Leu267	residue_name_number	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+73	79	Leu288	residue_name_number	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+124	130	Asn379	residue_name_number	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+132	138	Met431	residue_name_number	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+143	149	Met452	residue_name_number	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+153	157	MKP5	protein	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+158	160	CD	structure_element	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+213	237	hydrophobic interactions	bond_interaction	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+246	250	MKP5	protein	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+251	253	CD	structure_element	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+258	262	JNK1	protein	In addition, the key interacting residues of MKP7-CD, Phe215, Leu267 and Leu288, are replaced by less hydrophobic residues, Asn379, Met431 and Met452 in MKP5-CD (Fig. 5c), respectively, which may result in weaker hydrophobic interactions between MKP5-CD and JNK1.	RESULTS
+66	70	JNK1	protein	This is consistent with the experimental observation showing that JNK1 binds to MKP7-CD much more tightly than MKP5-CD (Km value of MKP5-CD for pJNK1 substrate is ∼20-fold higher than that of MKP7-CD).	RESULTS
+80	84	MKP7	protein	This is consistent with the experimental observation showing that JNK1 binds to MKP7-CD much more tightly than MKP5-CD (Km value of MKP5-CD for pJNK1 substrate is ∼20-fold higher than that of MKP7-CD).	RESULTS
+85	87	CD	structure_element	This is consistent with the experimental observation showing that JNK1 binds to MKP7-CD much more tightly than MKP5-CD (Km value of MKP5-CD for pJNK1 substrate is ∼20-fold higher than that of MKP7-CD).	RESULTS
+111	115	MKP5	protein	This is consistent with the experimental observation showing that JNK1 binds to MKP7-CD much more tightly than MKP5-CD (Km value of MKP5-CD for pJNK1 substrate is ∼20-fold higher than that of MKP7-CD).	RESULTS
+116	118	CD	structure_element	This is consistent with the experimental observation showing that JNK1 binds to MKP7-CD much more tightly than MKP5-CD (Km value of MKP5-CD for pJNK1 substrate is ∼20-fold higher than that of MKP7-CD).	RESULTS
+132	136	MKP5	protein	This is consistent with the experimental observation showing that JNK1 binds to MKP7-CD much more tightly than MKP5-CD (Km value of MKP5-CD for pJNK1 substrate is ∼20-fold higher than that of MKP7-CD).	RESULTS
+137	139	CD	structure_element	This is consistent with the experimental observation showing that JNK1 binds to MKP7-CD much more tightly than MKP5-CD (Km value of MKP5-CD for pJNK1 substrate is ∼20-fold higher than that of MKP7-CD).	RESULTS
+144	145	p	protein_state	This is consistent with the experimental observation showing that JNK1 binds to MKP7-CD much more tightly than MKP5-CD (Km value of MKP5-CD for pJNK1 substrate is ∼20-fold higher than that of MKP7-CD).	RESULTS
+145	149	JNK1	protein	This is consistent with the experimental observation showing that JNK1 binds to MKP7-CD much more tightly than MKP5-CD (Km value of MKP5-CD for pJNK1 substrate is ∼20-fold higher than that of MKP7-CD).	RESULTS
+192	196	MKP7	protein	This is consistent with the experimental observation showing that JNK1 binds to MKP7-CD much more tightly than MKP5-CD (Km value of MKP5-CD for pJNK1 substrate is ∼20-fold higher than that of MKP7-CD).	RESULTS
+197	199	CD	structure_element	This is consistent with the experimental observation showing that JNK1 binds to MKP7-CD much more tightly than MKP5-CD (Km value of MKP5-CD for pJNK1 substrate is ∼20-fold higher than that of MKP7-CD).	RESULTS
+4	9	MAPKs	protein_type	The MAPKs p38, ERK and JNK, are central to evolutionarily conserved signalling pathways that are present in all eukaryotic cells.	DISCUSS
+10	13	p38	protein_type	The MAPKs p38, ERK and JNK, are central to evolutionarily conserved signalling pathways that are present in all eukaryotic cells.	DISCUSS
+15	18	ERK	protein_type	The MAPKs p38, ERK and JNK, are central to evolutionarily conserved signalling pathways that are present in all eukaryotic cells.	DISCUSS
+23	26	JNK	protein_type	The MAPKs p38, ERK and JNK, are central to evolutionarily conserved signalling pathways that are present in all eukaryotic cells.	DISCUSS
+112	122	eukaryotic	taxonomy_domain	The MAPKs p38, ERK and JNK, are central to evolutionarily conserved signalling pathways that are present in all eukaryotic cells.	DISCUSS
+5	9	MAPK	protein_type	Each MAPK cascade is activated in response to a diverse array of extracellular signals and culminates in the dual-phosphorylation of a threonine and a tyrosine residue in the MAPK-activation loop.	DISCUSS
+109	129	dual-phosphorylation	ptm	Each MAPK cascade is activated in response to a diverse array of extracellular signals and culminates in the dual-phosphorylation of a threonine and a tyrosine residue in the MAPK-activation loop.	DISCUSS
+135	144	threonine	residue_name	Each MAPK cascade is activated in response to a diverse array of extracellular signals and culminates in the dual-phosphorylation of a threonine and a tyrosine residue in the MAPK-activation loop.	DISCUSS
+151	159	tyrosine	residue_name	Each MAPK cascade is activated in response to a diverse array of extracellular signals and culminates in the dual-phosphorylation of a threonine and a tyrosine residue in the MAPK-activation loop.	DISCUSS
+175	195	MAPK-activation loop	structure_element	Each MAPK cascade is activated in response to a diverse array of extracellular signals and culminates in the dual-phosphorylation of a threonine and a tyrosine residue in the MAPK-activation loop.	DISCUSS
+19	23	MAPK	protein_type	The propagation of MAPK signals is attenuated through the actions of the MKPs.	DISCUSS
+73	77	MKPs	protein_type	The propagation of MAPK signals is attenuated through the actions of the MKPs.	DISCUSS
+54	59	MAPKs	protein_type	Most studies have focused on the dephosphorylation of MAPKs by phosphatases containing the ‘kinase-interaction motif ' (D-motif), including a group of DUSPs (MKPs) and a distinct subfamily of tyrosine phosphatases (HePTP, STEP and PTP-SL).	DISCUSS
+63	75	phosphatases	protein_type	Most studies have focused on the dephosphorylation of MAPKs by phosphatases containing the ‘kinase-interaction motif ' (D-motif), including a group of DUSPs (MKPs) and a distinct subfamily of tyrosine phosphatases (HePTP, STEP and PTP-SL).	DISCUSS
+92	116	kinase-interaction motif	structure_element	Most studies have focused on the dephosphorylation of MAPKs by phosphatases containing the ‘kinase-interaction motif ' (D-motif), including a group of DUSPs (MKPs) and a distinct subfamily of tyrosine phosphatases (HePTP, STEP and PTP-SL).	DISCUSS
+120	127	D-motif	structure_element	Most studies have focused on the dephosphorylation of MAPKs by phosphatases containing the ‘kinase-interaction motif ' (D-motif), including a group of DUSPs (MKPs) and a distinct subfamily of tyrosine phosphatases (HePTP, STEP and PTP-SL).	DISCUSS
+151	156	DUSPs	protein_type	Most studies have focused on the dephosphorylation of MAPKs by phosphatases containing the ‘kinase-interaction motif ' (D-motif), including a group of DUSPs (MKPs) and a distinct subfamily of tyrosine phosphatases (HePTP, STEP and PTP-SL).	DISCUSS
+158	162	MKPs	protein_type	Most studies have focused on the dephosphorylation of MAPKs by phosphatases containing the ‘kinase-interaction motif ' (D-motif), including a group of DUSPs (MKPs) and a distinct subfamily of tyrosine phosphatases (HePTP, STEP and PTP-SL).	DISCUSS
+192	213	tyrosine phosphatases	protein_type	Most studies have focused on the dephosphorylation of MAPKs by phosphatases containing the ‘kinase-interaction motif ' (D-motif), including a group of DUSPs (MKPs) and a distinct subfamily of tyrosine phosphatases (HePTP, STEP and PTP-SL).	DISCUSS
+215	220	HePTP	protein	Most studies have focused on the dephosphorylation of MAPKs by phosphatases containing the ‘kinase-interaction motif ' (D-motif), including a group of DUSPs (MKPs) and a distinct subfamily of tyrosine phosphatases (HePTP, STEP and PTP-SL).	DISCUSS
+222	226	STEP	protein	Most studies have focused on the dephosphorylation of MAPKs by phosphatases containing the ‘kinase-interaction motif ' (D-motif), including a group of DUSPs (MKPs) and a distinct subfamily of tyrosine phosphatases (HePTP, STEP and PTP-SL).	DISCUSS
+231	237	PTP-SL	protein	Most studies have focused on the dephosphorylation of MAPKs by phosphatases containing the ‘kinase-interaction motif ' (D-motif), including a group of DUSPs (MKPs) and a distinct subfamily of tyrosine phosphatases (HePTP, STEP and PTP-SL).	DISCUSS
+0	18	Crystal structures	evidence	Crystal structures of ERK2 bound with the D-motif sequences derived from MKP3 and HePTP have been reported.	DISCUSS
+22	26	ERK2	protein	Crystal structures of ERK2 bound with the D-motif sequences derived from MKP3 and HePTP have been reported.	DISCUSS
+27	37	bound with	protein_state	Crystal structures of ERK2 bound with the D-motif sequences derived from MKP3 and HePTP have been reported.	DISCUSS
+42	49	D-motif	structure_element	Crystal structures of ERK2 bound with the D-motif sequences derived from MKP3 and HePTP have been reported.	DISCUSS
+73	77	MKP3	protein	Crystal structures of ERK2 bound with the D-motif sequences derived from MKP3 and HePTP have been reported.	DISCUSS
+82	87	HePTP	protein	Crystal structures of ERK2 bound with the D-motif sequences derived from MKP3 and HePTP have been reported.	DISCUSS
+6	16	structures	evidence	These structures revealed that linear docking motifs in interacting proteins bind to a common docking site on MAPKs outside the kinase active site.	DISCUSS
+31	52	linear docking motifs	structure_element	These structures revealed that linear docking motifs in interacting proteins bind to a common docking site on MAPKs outside the kinase active site.	DISCUSS
+94	106	docking site	site	These structures revealed that linear docking motifs in interacting proteins bind to a common docking site on MAPKs outside the kinase active site.	DISCUSS
+110	115	MAPKs	protein_type	These structures revealed that linear docking motifs in interacting proteins bind to a common docking site on MAPKs outside the kinase active site.	DISCUSS
+128	134	kinase	protein_type	These structures revealed that linear docking motifs in interacting proteins bind to a common docking site on MAPKs outside the kinase active site.	DISCUSS
+135	146	active site	site	These structures revealed that linear docking motifs in interacting proteins bind to a common docking site on MAPKs outside the kinase active site.	DISCUSS
+52	59	D-motif	structure_element	The particular amino acids and their spacing within D-motif sequences and amino acid composition of the docking sites on MAPKs appear to determine the specificity of D-motifs for individual MAPKs.	DISCUSS
+104	117	docking sites	site	The particular amino acids and their spacing within D-motif sequences and amino acid composition of the docking sites on MAPKs appear to determine the specificity of D-motifs for individual MAPKs.	DISCUSS
+121	126	MAPKs	protein_type	The particular amino acids and their spacing within D-motif sequences and amino acid composition of the docking sites on MAPKs appear to determine the specificity of D-motifs for individual MAPKs.	DISCUSS
+166	174	D-motifs	structure_element	The particular amino acids and their spacing within D-motif sequences and amino acid composition of the docking sites on MAPKs appear to determine the specificity of D-motifs for individual MAPKs.	DISCUSS
+190	195	MAPKs	protein_type	The particular amino acids and their spacing within D-motif sequences and amino acid composition of the docking sites on MAPKs appear to determine the specificity of D-motifs for individual MAPKs.	DISCUSS
+14	31	crystal structure	evidence	Recently, the crystal structure of a complex between the KBD of MKP5 and p38α has been obtained.	DISCUSS
+57	60	KBD	structure_element	Recently, the crystal structure of a complex between the KBD of MKP5 and p38α has been obtained.	DISCUSS
+64	68	MKP5	protein	Recently, the crystal structure of a complex between the KBD of MKP5 and p38α has been obtained.	DISCUSS
+73	77	p38α	protein	Recently, the crystal structure of a complex between the KBD of MKP5 and p38α has been obtained.	DISCUSS
+58	62	MKP5	protein	This complex has revealed a distinct interaction mode for MKP5.	DISCUSS
+4	7	KBD	structure_element	The KBD of MKP5 binds to p38α in the opposite polypeptide direction compared with how the D-motif of MKP3 binds to ERK2.	DISCUSS
+11	15	MKP5	protein	The KBD of MKP5 binds to p38α in the opposite polypeptide direction compared with how the D-motif of MKP3 binds to ERK2.	DISCUSS
+25	29	p38α	protein	The KBD of MKP5 binds to p38α in the opposite polypeptide direction compared with how the D-motif of MKP3 binds to ERK2.	DISCUSS
+90	97	D-motif	structure_element	The KBD of MKP5 binds to p38α in the opposite polypeptide direction compared with how the D-motif of MKP3 binds to ERK2.	DISCUSS
+101	105	MKP3	protein	The KBD of MKP5 binds to p38α in the opposite polypeptide direction compared with how the D-motif of MKP3 binds to ERK2.	DISCUSS
+115	119	ERK2	protein	The KBD of MKP5 binds to p38α in the opposite polypeptide direction compared with how the D-motif of MKP3 binds to ERK2.	DISCUSS
+29	49	D-motif-binding mode	site	In contrast to the canonical D-motif-binding mode, separate helices, α2 and α3′, in the KBD of MKP5 engage the p38α-docking site.	DISCUSS
+60	67	helices	structure_element	In contrast to the canonical D-motif-binding mode, separate helices, α2 and α3′, in the KBD of MKP5 engage the p38α-docking site.	DISCUSS
+69	71	α2	structure_element	In contrast to the canonical D-motif-binding mode, separate helices, α2 and α3′, in the KBD of MKP5 engage the p38α-docking site.	DISCUSS
+76	79	α3′	structure_element	In contrast to the canonical D-motif-binding mode, separate helices, α2 and α3′, in the KBD of MKP5 engage the p38α-docking site.	DISCUSS
+88	91	KBD	structure_element	In contrast to the canonical D-motif-binding mode, separate helices, α2 and α3′, in the KBD of MKP5 engage the p38α-docking site.	DISCUSS
+95	99	MKP5	protein	In contrast to the canonical D-motif-binding mode, separate helices, α2 and α3′, in the KBD of MKP5 engage the p38α-docking site.	DISCUSS
+111	128	p38α-docking site	site	In contrast to the canonical D-motif-binding mode, separate helices, α2 and α3′, in the KBD of MKP5 engage the p38α-docking site.	DISCUSS
+8	42	structural and biochemical studies	experimental_method	Further structural and biochemical studies indicate that KBD of MKP7 may interact with p38α in a similar manner to that of MKP5.	DISCUSS
+57	60	KBD	structure_element	Further structural and biochemical studies indicate that KBD of MKP7 may interact with p38α in a similar manner to that of MKP5.	DISCUSS
+64	68	MKP7	protein	Further structural and biochemical studies indicate that KBD of MKP7 may interact with p38α in a similar manner to that of MKP5.	DISCUSS
+87	91	p38α	protein	Further structural and biochemical studies indicate that KBD of MKP7 may interact with p38α in a similar manner to that of MKP5.	DISCUSS
+123	127	MKP5	protein	Further structural and biochemical studies indicate that KBD of MKP7 may interact with p38α in a similar manner to that of MKP5.	DISCUSS
+15	19	MKP5	protein	In contrast to MKP5, removal of the KBD domain from MKP7 does not drastically affect enzyme catalysis, and the kinetic parameters of MKP7-CD for p38α substrate are very similar to those for JNK1 substrate.	DISCUSS
+21	31	removal of	experimental_method	In contrast to MKP5, removal of the KBD domain from MKP7 does not drastically affect enzyme catalysis, and the kinetic parameters of MKP7-CD for p38α substrate are very similar to those for JNK1 substrate.	DISCUSS
+36	39	KBD	structure_element	In contrast to MKP5, removal of the KBD domain from MKP7 does not drastically affect enzyme catalysis, and the kinetic parameters of MKP7-CD for p38α substrate are very similar to those for JNK1 substrate.	DISCUSS
+52	56	MKP7	protein	In contrast to MKP5, removal of the KBD domain from MKP7 does not drastically affect enzyme catalysis, and the kinetic parameters of MKP7-CD for p38α substrate are very similar to those for JNK1 substrate.	DISCUSS
+133	137	MKP7	protein	In contrast to MKP5, removal of the KBD domain from MKP7 does not drastically affect enzyme catalysis, and the kinetic parameters of MKP7-CD for p38α substrate are very similar to those for JNK1 substrate.	DISCUSS
+138	140	CD	structure_element	In contrast to MKP5, removal of the KBD domain from MKP7 does not drastically affect enzyme catalysis, and the kinetic parameters of MKP7-CD for p38α substrate are very similar to those for JNK1 substrate.	DISCUSS
+145	149	p38α	protein	In contrast to MKP5, removal of the KBD domain from MKP7 does not drastically affect enzyme catalysis, and the kinetic parameters of MKP7-CD for p38α substrate are very similar to those for JNK1 substrate.	DISCUSS
+190	194	JNK1	protein	In contrast to MKP5, removal of the KBD domain from MKP7 does not drastically affect enzyme catalysis, and the kinetic parameters of MKP7-CD for p38α substrate are very similar to those for JNK1 substrate.	DISCUSS
+43	47	MKP7	protein	Taken together, these results suggest that MKP7 utilizes a bipartite recognition mechanism to achieve the efficiency and fidelity of p38α signalling.	DISCUSS
+133	137	p38α	protein	Taken together, these results suggest that MKP7 utilizes a bipartite recognition mechanism to achieve the efficiency and fidelity of p38α signalling.	DISCUSS
+4	8	MKP7	protein	The MKP7-KBD docks to the D-site located on the back side of the p38α catalytic pocket for high-affinity association, whereas the interaction of the MKP7-CD with another p38α structural region, which is close to the activation loop, may not only stabilize binding but also provide contacts crucial for organizing the MKP7 active site with respect to the phosphoreceptor in the p38α substrate for efficient dephosphorylation.	DISCUSS
+9	12	KBD	structure_element	The MKP7-KBD docks to the D-site located on the back side of the p38α catalytic pocket for high-affinity association, whereas the interaction of the MKP7-CD with another p38α structural region, which is close to the activation loop, may not only stabilize binding but also provide contacts crucial for organizing the MKP7 active site with respect to the phosphoreceptor in the p38α substrate for efficient dephosphorylation.	DISCUSS
+26	32	D-site	site	The MKP7-KBD docks to the D-site located on the back side of the p38α catalytic pocket for high-affinity association, whereas the interaction of the MKP7-CD with another p38α structural region, which is close to the activation loop, may not only stabilize binding but also provide contacts crucial for organizing the MKP7 active site with respect to the phosphoreceptor in the p38α substrate for efficient dephosphorylation.	DISCUSS
+65	69	p38α	protein	The MKP7-KBD docks to the D-site located on the back side of the p38α catalytic pocket for high-affinity association, whereas the interaction of the MKP7-CD with another p38α structural region, which is close to the activation loop, may not only stabilize binding but also provide contacts crucial for organizing the MKP7 active site with respect to the phosphoreceptor in the p38α substrate for efficient dephosphorylation.	DISCUSS
+70	86	catalytic pocket	site	The MKP7-KBD docks to the D-site located on the back side of the p38α catalytic pocket for high-affinity association, whereas the interaction of the MKP7-CD with another p38α structural region, which is close to the activation loop, may not only stabilize binding but also provide contacts crucial for organizing the MKP7 active site with respect to the phosphoreceptor in the p38α substrate for efficient dephosphorylation.	DISCUSS
+149	153	MKP7	protein	The MKP7-KBD docks to the D-site located on the back side of the p38α catalytic pocket for high-affinity association, whereas the interaction of the MKP7-CD with another p38α structural region, which is close to the activation loop, may not only stabilize binding but also provide contacts crucial for organizing the MKP7 active site with respect to the phosphoreceptor in the p38α substrate for efficient dephosphorylation.	DISCUSS
+154	156	CD	structure_element	The MKP7-KBD docks to the D-site located on the back side of the p38α catalytic pocket for high-affinity association, whereas the interaction of the MKP7-CD with another p38α structural region, which is close to the activation loop, may not only stabilize binding but also provide contacts crucial for organizing the MKP7 active site with respect to the phosphoreceptor in the p38α substrate for efficient dephosphorylation.	DISCUSS
+170	174	p38α	protein	The MKP7-KBD docks to the D-site located on the back side of the p38α catalytic pocket for high-affinity association, whereas the interaction of the MKP7-CD with another p38α structural region, which is close to the activation loop, may not only stabilize binding but also provide contacts crucial for organizing the MKP7 active site with respect to the phosphoreceptor in the p38α substrate for efficient dephosphorylation.	DISCUSS
+216	231	activation loop	structure_element	The MKP7-KBD docks to the D-site located on the back side of the p38α catalytic pocket for high-affinity association, whereas the interaction of the MKP7-CD with another p38α structural region, which is close to the activation loop, may not only stabilize binding but also provide contacts crucial for organizing the MKP7 active site with respect to the phosphoreceptor in the p38α substrate for efficient dephosphorylation.	DISCUSS
+317	321	MKP7	protein	The MKP7-KBD docks to the D-site located on the back side of the p38α catalytic pocket for high-affinity association, whereas the interaction of the MKP7-CD with another p38α structural region, which is close to the activation loop, may not only stabilize binding but also provide contacts crucial for organizing the MKP7 active site with respect to the phosphoreceptor in the p38α substrate for efficient dephosphorylation.	DISCUSS
+322	333	active site	site	The MKP7-KBD docks to the D-site located on the back side of the p38α catalytic pocket for high-affinity association, whereas the interaction of the MKP7-CD with another p38α structural region, which is close to the activation loop, may not only stabilize binding but also provide contacts crucial for organizing the MKP7 active site with respect to the phosphoreceptor in the p38α substrate for efficient dephosphorylation.	DISCUSS
+377	381	p38α	protein	The MKP7-KBD docks to the D-site located on the back side of the p38α catalytic pocket for high-affinity association, whereas the interaction of the MKP7-CD with another p38α structural region, which is close to the activation loop, may not only stabilize binding but also provide contacts crucial for organizing the MKP7 active site with respect to the phosphoreceptor in the p38α substrate for efficient dephosphorylation.	DISCUSS
+29	35	D-site	site	In addition to the canonical D-site, the MAPK ERK2 contains a second binding site utilized by transcription factor substrates and phosphatases, the FXF-motif-binding site (also called F-site), that is exposed in active ERK2 and the D-motif peptide-induced conformation of MAPKs.	DISCUSS
+41	45	MAPK	protein_type	In addition to the canonical D-site, the MAPK ERK2 contains a second binding site utilized by transcription factor substrates and phosphatases, the FXF-motif-binding site (also called F-site), that is exposed in active ERK2 and the D-motif peptide-induced conformation of MAPKs.	DISCUSS
+46	50	ERK2	protein	In addition to the canonical D-site, the MAPK ERK2 contains a second binding site utilized by transcription factor substrates and phosphatases, the FXF-motif-binding site (also called F-site), that is exposed in active ERK2 and the D-motif peptide-induced conformation of MAPKs.	DISCUSS
+62	81	second binding site	site	In addition to the canonical D-site, the MAPK ERK2 contains a second binding site utilized by transcription factor substrates and phosphatases, the FXF-motif-binding site (also called F-site), that is exposed in active ERK2 and the D-motif peptide-induced conformation of MAPKs.	DISCUSS
+130	142	phosphatases	protein_type	In addition to the canonical D-site, the MAPK ERK2 contains a second binding site utilized by transcription factor substrates and phosphatases, the FXF-motif-binding site (also called F-site), that is exposed in active ERK2 and the D-motif peptide-induced conformation of MAPKs.	DISCUSS
+148	170	FXF-motif-binding site	site	In addition to the canonical D-site, the MAPK ERK2 contains a second binding site utilized by transcription factor substrates and phosphatases, the FXF-motif-binding site (also called F-site), that is exposed in active ERK2 and the D-motif peptide-induced conformation of MAPKs.	DISCUSS
+184	190	F-site	site	In addition to the canonical D-site, the MAPK ERK2 contains a second binding site utilized by transcription factor substrates and phosphatases, the FXF-motif-binding site (also called F-site), that is exposed in active ERK2 and the D-motif peptide-induced conformation of MAPKs.	DISCUSS
+212	218	active	protein_state	In addition to the canonical D-site, the MAPK ERK2 contains a second binding site utilized by transcription factor substrates and phosphatases, the FXF-motif-binding site (also called F-site), that is exposed in active ERK2 and the D-motif peptide-induced conformation of MAPKs.	DISCUSS
+219	223	ERK2	protein	In addition to the canonical D-site, the MAPK ERK2 contains a second binding site utilized by transcription factor substrates and phosphatases, the FXF-motif-binding site (also called F-site), that is exposed in active ERK2 and the D-motif peptide-induced conformation of MAPKs.	DISCUSS
+232	239	D-motif	structure_element	In addition to the canonical D-site, the MAPK ERK2 contains a second binding site utilized by transcription factor substrates and phosphatases, the FXF-motif-binding site (also called F-site), that is exposed in active ERK2 and the D-motif peptide-induced conformation of MAPKs.	DISCUSS
+272	277	MAPKs	protein_type	In addition to the canonical D-site, the MAPK ERK2 contains a second binding site utilized by transcription factor substrates and phosphatases, the FXF-motif-binding site (also called F-site), that is exposed in active ERK2 and the D-motif peptide-induced conformation of MAPKs.	DISCUSS
+5	21	hydrophobic site	site	This hydrophobic site was first identified by changes in deuterium exchange profiles, and is near the MAPK insertion and helix αG. Interestingly, many of the equivalent residues in JNK1, important for MKP7-CD recognition, are also used for substrate binding by ERK2 (ref.), indicating that this site is overlapped with the DEF-site previously identified in ERK2 (Fig. 5d).	DISCUSS
+46	84	changes in deuterium exchange profiles	evidence	This hydrophobic site was first identified by changes in deuterium exchange profiles, and is near the MAPK insertion and helix αG. Interestingly, many of the equivalent residues in JNK1, important for MKP7-CD recognition, are also used for substrate binding by ERK2 (ref.), indicating that this site is overlapped with the DEF-site previously identified in ERK2 (Fig. 5d).	DISCUSS
+102	116	MAPK insertion	structure_element	This hydrophobic site was first identified by changes in deuterium exchange profiles, and is near the MAPK insertion and helix αG. Interestingly, many of the equivalent residues in JNK1, important for MKP7-CD recognition, are also used for substrate binding by ERK2 (ref.), indicating that this site is overlapped with the DEF-site previously identified in ERK2 (Fig. 5d).	DISCUSS
+121	126	helix	structure_element	This hydrophobic site was first identified by changes in deuterium exchange profiles, and is near the MAPK insertion and helix αG. Interestingly, many of the equivalent residues in JNK1, important for MKP7-CD recognition, are also used for substrate binding by ERK2 (ref.), indicating that this site is overlapped with the DEF-site previously identified in ERK2 (Fig. 5d).	DISCUSS
+127	129	αG	structure_element	This hydrophobic site was first identified by changes in deuterium exchange profiles, and is near the MAPK insertion and helix αG. Interestingly, many of the equivalent residues in JNK1, important for MKP7-CD recognition, are also used for substrate binding by ERK2 (ref.), indicating that this site is overlapped with the DEF-site previously identified in ERK2 (Fig. 5d).	DISCUSS
+181	185	JNK1	protein	This hydrophobic site was first identified by changes in deuterium exchange profiles, and is near the MAPK insertion and helix αG. Interestingly, many of the equivalent residues in JNK1, important for MKP7-CD recognition, are also used for substrate binding by ERK2 (ref.), indicating that this site is overlapped with the DEF-site previously identified in ERK2 (Fig. 5d).	DISCUSS
+201	205	MKP7	protein	This hydrophobic site was first identified by changes in deuterium exchange profiles, and is near the MAPK insertion and helix αG. Interestingly, many of the equivalent residues in JNK1, important for MKP7-CD recognition, are also used for substrate binding by ERK2 (ref.), indicating that this site is overlapped with the DEF-site previously identified in ERK2 (Fig. 5d).	DISCUSS
+206	208	CD	structure_element	This hydrophobic site was first identified by changes in deuterium exchange profiles, and is near the MAPK insertion and helix αG. Interestingly, many of the equivalent residues in JNK1, important for MKP7-CD recognition, are also used for substrate binding by ERK2 (ref.), indicating that this site is overlapped with the DEF-site previously identified in ERK2 (Fig. 5d).	DISCUSS
+261	265	ERK2	protein	This hydrophobic site was first identified by changes in deuterium exchange profiles, and is near the MAPK insertion and helix αG. Interestingly, many of the equivalent residues in JNK1, important for MKP7-CD recognition, are also used for substrate binding by ERK2 (ref.), indicating that this site is overlapped with the DEF-site previously identified in ERK2 (Fig. 5d).	DISCUSS
+323	331	DEF-site	site	This hydrophobic site was first identified by changes in deuterium exchange profiles, and is near the MAPK insertion and helix αG. Interestingly, many of the equivalent residues in JNK1, important for MKP7-CD recognition, are also used for substrate binding by ERK2 (ref.), indicating that this site is overlapped with the DEF-site previously identified in ERK2 (Fig. 5d).	DISCUSS
+357	361	ERK2	protein	This hydrophobic site was first identified by changes in deuterium exchange profiles, and is near the MAPK insertion and helix αG. Interestingly, many of the equivalent residues in JNK1, important for MKP7-CD recognition, are also used for substrate binding by ERK2 (ref.), indicating that this site is overlapped with the DEF-site previously identified in ERK2 (Fig. 5d).	DISCUSS
+0	4	MKP3	protein	MKP3 is highly specific in dephosphorylating and inactivating ERK2, and the phosphatase activity of the MKP3-catalysed pNPP reaction can be markedly increased in the presence of ERK2 (refs).	DISCUSS
+62	66	ERK2	protein	MKP3 is highly specific in dephosphorylating and inactivating ERK2, and the phosphatase activity of the MKP3-catalysed pNPP reaction can be markedly increased in the presence of ERK2 (refs).	DISCUSS
+104	108	MKP3	protein	MKP3 is highly specific in dephosphorylating and inactivating ERK2, and the phosphatase activity of the MKP3-catalysed pNPP reaction can be markedly increased in the presence of ERK2 (refs).	DISCUSS
+119	123	pNPP	chemical	MKP3 is highly specific in dephosphorylating and inactivating ERK2, and the phosphatase activity of the MKP3-catalysed pNPP reaction can be markedly increased in the presence of ERK2 (refs).	DISCUSS
+166	177	presence of	protein_state	MKP3 is highly specific in dephosphorylating and inactivating ERK2, and the phosphatase activity of the MKP3-catalysed pNPP reaction can be markedly increased in the presence of ERK2 (refs).	DISCUSS
+178	182	ERK2	protein	MKP3 is highly specific in dephosphorylating and inactivating ERK2, and the phosphatase activity of the MKP3-catalysed pNPP reaction can be markedly increased in the presence of ERK2 (refs).	DISCUSS
+0	18	Sequence alignment	experimental_method	Sequence alignment of all MKPs reveals a high degree of conservation of residues surrounding the interacting region observed in JNK1–MKP7-CD complex (Supplementary Fig. 5).	DISCUSS
+26	30	MKPs	protein_type	Sequence alignment of all MKPs reveals a high degree of conservation of residues surrounding the interacting region observed in JNK1–MKP7-CD complex (Supplementary Fig. 5).	DISCUSS
+97	115	interacting region	site	Sequence alignment of all MKPs reveals a high degree of conservation of residues surrounding the interacting region observed in JNK1–MKP7-CD complex (Supplementary Fig. 5).	DISCUSS
+128	140	JNK1–MKP7-CD	complex_assembly	Sequence alignment of all MKPs reveals a high degree of conservation of residues surrounding the interacting region observed in JNK1–MKP7-CD complex (Supplementary Fig. 5).	DISCUSS
+48	64	catalytic domain	structure_element	Therefore, it is tempting to speculate that the catalytic domain of MKP3 may bind to ERK2 in a manner analogous to the way by which MKP7-CD binds to JNK1.	DISCUSS
+68	72	MKP3	protein	Therefore, it is tempting to speculate that the catalytic domain of MKP3 may bind to ERK2 in a manner analogous to the way by which MKP7-CD binds to JNK1.	DISCUSS
+85	89	ERK2	protein	Therefore, it is tempting to speculate that the catalytic domain of MKP3 may bind to ERK2 in a manner analogous to the way by which MKP7-CD binds to JNK1.	DISCUSS
+132	136	MKP7	protein	Therefore, it is tempting to speculate that the catalytic domain of MKP3 may bind to ERK2 in a manner analogous to the way by which MKP7-CD binds to JNK1.	DISCUSS
+137	139	CD	structure_element	Therefore, it is tempting to speculate that the catalytic domain of MKP3 may bind to ERK2 in a manner analogous to the way by which MKP7-CD binds to JNK1.	DISCUSS
+149	153	JNK1	protein	Therefore, it is tempting to speculate that the catalytic domain of MKP3 may bind to ERK2 in a manner analogous to the way by which MKP7-CD binds to JNK1.	DISCUSS
+67	71	ERK2	protein	A comprehensive examination of the molecular basis of the specific ERK2 recognition by MKP3 is underway.	DISCUSS
+87	91	MKP3	protein	A comprehensive examination of the molecular basis of the specific ERK2 recognition by MKP3 is underway.	DISCUSS
+98	110	JNK1–MKP7-CD	complex_assembly	The ongoing work demonstrates that although the overall interaction modes are similar between the JNK1–MKP7-CD and ERK2–MKP3-CD complexes, the ERK2–MKP3-CD interaction is less extensive and helix α4 from MKP3-CD does not interact directly with ERK2.	DISCUSS
+115	127	ERK2–MKP3-CD	complex_assembly	The ongoing work demonstrates that although the overall interaction modes are similar between the JNK1–MKP7-CD and ERK2–MKP3-CD complexes, the ERK2–MKP3-CD interaction is less extensive and helix α4 from MKP3-CD does not interact directly with ERK2.	DISCUSS
+143	155	ERK2–MKP3-CD	complex_assembly	The ongoing work demonstrates that although the overall interaction modes are similar between the JNK1–MKP7-CD and ERK2–MKP3-CD complexes, the ERK2–MKP3-CD interaction is less extensive and helix α4 from MKP3-CD does not interact directly with ERK2.	DISCUSS
+190	195	helix	structure_element	The ongoing work demonstrates that although the overall interaction modes are similar between the JNK1–MKP7-CD and ERK2–MKP3-CD complexes, the ERK2–MKP3-CD interaction is less extensive and helix α4 from MKP3-CD does not interact directly with ERK2.	DISCUSS
+196	198	α4	structure_element	The ongoing work demonstrates that although the overall interaction modes are similar between the JNK1–MKP7-CD and ERK2–MKP3-CD complexes, the ERK2–MKP3-CD interaction is less extensive and helix α4 from MKP3-CD does not interact directly with ERK2.	DISCUSS
+204	208	MKP3	protein	The ongoing work demonstrates that although the overall interaction modes are similar between the JNK1–MKP7-CD and ERK2–MKP3-CD complexes, the ERK2–MKP3-CD interaction is less extensive and helix α4 from MKP3-CD does not interact directly with ERK2.	DISCUSS
+209	211	CD	structure_element	The ongoing work demonstrates that although the overall interaction modes are similar between the JNK1–MKP7-CD and ERK2–MKP3-CD complexes, the ERK2–MKP3-CD interaction is less extensive and helix α4 from MKP3-CD does not interact directly with ERK2.	DISCUSS
+244	248	ERK2	protein	The ongoing work demonstrates that although the overall interaction modes are similar between the JNK1–MKP7-CD and ERK2–MKP3-CD complexes, the ERK2–MKP3-CD interaction is less extensive and helix α4 from MKP3-CD does not interact directly with ERK2.	DISCUSS
+4	13	FXF-motif	structure_element	The FXF-motif-mediated interaction is critical for both pERK2 inactivation and ERK2-induced MKP3 activation (manuscript in preparation).	DISCUSS
+56	57	p	protein_state	The FXF-motif-mediated interaction is critical for both pERK2 inactivation and ERK2-induced MKP3 activation (manuscript in preparation).	DISCUSS
+57	61	ERK2	protein	The FXF-motif-mediated interaction is critical for both pERK2 inactivation and ERK2-induced MKP3 activation (manuscript in preparation).	DISCUSS
+79	83	ERK2	protein	The FXF-motif-mediated interaction is critical for both pERK2 inactivation and ERK2-induced MKP3 activation (manuscript in preparation).	DISCUSS
+92	96	MKP3	protein	The FXF-motif-mediated interaction is critical for both pERK2 inactivation and ERK2-induced MKP3 activation (manuscript in preparation).	DISCUSS
+33	42	structure	evidence	In summary, we have resolved the structure of JNK1 in complex with the catalytic domain of MKP7.	DISCUSS
+46	50	JNK1	protein	In summary, we have resolved the structure of JNK1 in complex with the catalytic domain of MKP7.	DISCUSS
+51	66	in complex with	protein_state	In summary, we have resolved the structure of JNK1 in complex with the catalytic domain of MKP7.	DISCUSS
+71	87	catalytic domain	structure_element	In summary, we have resolved the structure of JNK1 in complex with the catalytic domain of MKP7.	DISCUSS
+91	95	MKP7	protein	In summary, we have resolved the structure of JNK1 in complex with the catalytic domain of MKP7.	DISCUSS
+5	14	structure	evidence	This structure reveals an FXF-docking interaction mode between MAPK and MKP.	DISCUSS
+26	54	FXF-docking interaction mode	site	This structure reveals an FXF-docking interaction mode between MAPK and MKP.	DISCUSS
+63	67	MAPK	protein_type	This structure reveals an FXF-docking interaction mode between MAPK and MKP.	DISCUSS
+72	75	MKP	protein_type	This structure reveals an FXF-docking interaction mode between MAPK and MKP.	DISCUSS
+13	41	biochemical characterization	experimental_method	Results from biochemical characterization of the Phe285 and Phe287 MKP7 mutants combined with structural information support the conclusion that the two Phe residues serve different roles in the catalytic reaction.	DISCUSS
+49	55	Phe285	residue_name_number	Results from biochemical characterization of the Phe285 and Phe287 MKP7 mutants combined with structural information support the conclusion that the two Phe residues serve different roles in the catalytic reaction.	DISCUSS
+60	66	Phe287	residue_name_number	Results from biochemical characterization of the Phe285 and Phe287 MKP7 mutants combined with structural information support the conclusion that the two Phe residues serve different roles in the catalytic reaction.	DISCUSS
+67	71	MKP7	protein	Results from biochemical characterization of the Phe285 and Phe287 MKP7 mutants combined with structural information support the conclusion that the two Phe residues serve different roles in the catalytic reaction.	DISCUSS
+72	79	mutants	protein_state	Results from biochemical characterization of the Phe285 and Phe287 MKP7 mutants combined with structural information support the conclusion that the two Phe residues serve different roles in the catalytic reaction.	DISCUSS
+94	116	structural information	evidence	Results from biochemical characterization of the Phe285 and Phe287 MKP7 mutants combined with structural information support the conclusion that the two Phe residues serve different roles in the catalytic reaction.	DISCUSS
+153	156	Phe	residue_name	Results from biochemical characterization of the Phe285 and Phe287 MKP7 mutants combined with structural information support the conclusion that the two Phe residues serve different roles in the catalytic reaction.	DISCUSS
+0	6	Phe285	residue_name_number	Phe285 is essential for JNK1 substrate binding, whereas Phe287 plays a role for the precise alignment of active-site residues, which are important for transition-state stabilization.	DISCUSS
+24	28	JNK1	protein	Phe285 is essential for JNK1 substrate binding, whereas Phe287 plays a role for the precise alignment of active-site residues, which are important for transition-state stabilization.	DISCUSS
+56	62	Phe287	residue_name_number	Phe285 is essential for JNK1 substrate binding, whereas Phe287 plays a role for the precise alignment of active-site residues, which are important for transition-state stabilization.	DISCUSS
+105	125	active-site residues	site	Phe285 is essential for JNK1 substrate binding, whereas Phe287 plays a role for the precise alignment of active-site residues, which are important for transition-state stabilization.	DISCUSS
+22	36	FXF-type motif	structure_element	This newly identified FXF-type motif is present in all MKPs, except that the residue at the first position in MKP5 is an equivalent hydrophobic leucine residue (see also Fig. 7f,g), suggesting that these two Phe residues would play a similar role in facilitating substrate recognition and catalysis, respectively.	DISCUSS
+55	59	MKPs	protein_type	This newly identified FXF-type motif is present in all MKPs, except that the residue at the first position in MKP5 is an equivalent hydrophobic leucine residue (see also Fig. 7f,g), suggesting that these two Phe residues would play a similar role in facilitating substrate recognition and catalysis, respectively.	DISCUSS
+110	114	MKP5	protein	This newly identified FXF-type motif is present in all MKPs, except that the residue at the first position in MKP5 is an equivalent hydrophobic leucine residue (see also Fig. 7f,g), suggesting that these two Phe residues would play a similar role in facilitating substrate recognition and catalysis, respectively.	DISCUSS
+144	151	leucine	residue_name	This newly identified FXF-type motif is present in all MKPs, except that the residue at the first position in MKP5 is an equivalent hydrophobic leucine residue (see also Fig. 7f,g), suggesting that these two Phe residues would play a similar role in facilitating substrate recognition and catalysis, respectively.	DISCUSS
+208	211	Phe	residue_name	This newly identified FXF-type motif is present in all MKPs, except that the residue at the first position in MKP5 is an equivalent hydrophobic leucine residue (see also Fig. 7f,g), suggesting that these two Phe residues would play a similar role in facilitating substrate recognition and catalysis, respectively.	DISCUSS
+24	27	MKP	protein_type	An important feature of MKP–JNK1 interactions is that MKP7 or MKP5 only interact with the F-site of JNK1.	DISCUSS
+28	32	JNK1	protein	An important feature of MKP–JNK1 interactions is that MKP7 or MKP5 only interact with the F-site of JNK1.	DISCUSS
+54	58	MKP7	protein	An important feature of MKP–JNK1 interactions is that MKP7 or MKP5 only interact with the F-site of JNK1.	DISCUSS
+62	66	MKP5	protein	An important feature of MKP–JNK1 interactions is that MKP7 or MKP5 only interact with the F-site of JNK1.	DISCUSS
+90	96	F-site	site	An important feature of MKP–JNK1 interactions is that MKP7 or MKP5 only interact with the F-site of JNK1.	DISCUSS
+100	104	JNK1	protein	An important feature of MKP–JNK1 interactions is that MKP7 or MKP5 only interact with the F-site of JNK1.	DISCUSS
+33	37	JNK1	protein	One possible explanation is that JNK1 needs to use the D-site to interact with JIP-1, a scaffold protein for JNK signalling.	DISCUSS
+55	61	D-site	site	One possible explanation is that JNK1 needs to use the D-site to interact with JIP-1, a scaffold protein for JNK signalling.	DISCUSS
+79	84	JIP-1	protein	One possible explanation is that JNK1 needs to use the D-site to interact with JIP-1, a scaffold protein for JNK signalling.	DISCUSS
+109	112	JNK	protein_type	One possible explanation is that JNK1 needs to use the D-site to interact with JIP-1, a scaffold protein for JNK signalling.	DISCUSS
+15	33	JNK-binding domain	structure_element	The N-terminal JNK-binding domain of JIP-1 interacts with the D-site on JNK and this interaction is required for JIP-1-mediated enhancement of JNK activation.	DISCUSS
+37	42	JIP-1	protein	The N-terminal JNK-binding domain of JIP-1 interacts with the D-site on JNK and this interaction is required for JIP-1-mediated enhancement of JNK activation.	DISCUSS
+62	68	D-site	site	The N-terminal JNK-binding domain of JIP-1 interacts with the D-site on JNK and this interaction is required for JIP-1-mediated enhancement of JNK activation.	DISCUSS
+72	75	JNK	protein_type	The N-terminal JNK-binding domain of JIP-1 interacts with the D-site on JNK and this interaction is required for JIP-1-mediated enhancement of JNK activation.	DISCUSS
+113	118	JIP-1	protein	The N-terminal JNK-binding domain of JIP-1 interacts with the D-site on JNK and this interaction is required for JIP-1-mediated enhancement of JNK activation.	DISCUSS
+143	146	JNK	protein_type	The N-terminal JNK-binding domain of JIP-1 interacts with the D-site on JNK and this interaction is required for JIP-1-mediated enhancement of JNK activation.	DISCUSS
+13	18	JIP-1	protein	In addition, JIP-1 can also associate with MKP7 via the C-terminal region of MKP7 (ref.).	DISCUSS
+43	47	MKP7	protein	In addition, JIP-1 can also associate with MKP7 via the C-terminal region of MKP7 (ref.).	DISCUSS
+56	73	C-terminal region	structure_element	In addition, JIP-1 can also associate with MKP7 via the C-terminal region of MKP7 (ref.).	DISCUSS
+77	81	MKP7	protein	In addition, JIP-1 can also associate with MKP7 via the C-terminal region of MKP7 (ref.).	DISCUSS
+5	9	MKP7	protein	When MKP7 is bound to JIP-1, it reduces JNK activation, leading to reduced phosphorylation of the JNK target c-Jun.	DISCUSS
+13	21	bound to	protein_state	When MKP7 is bound to JIP-1, it reduces JNK activation, leading to reduced phosphorylation of the JNK target c-Jun.	DISCUSS
+22	27	JIP-1	protein	When MKP7 is bound to JIP-1, it reduces JNK activation, leading to reduced phosphorylation of the JNK target c-Jun.	DISCUSS
+40	43	JNK	protein_type	When MKP7 is bound to JIP-1, it reduces JNK activation, leading to reduced phosphorylation of the JNK target c-Jun.	DISCUSS
+98	101	JNK	protein_type	When MKP7 is bound to JIP-1, it reduces JNK activation, leading to reduced phosphorylation of the JNK target c-Jun.	DISCUSS
+109	114	c-Jun	protein_type	When MKP7 is bound to JIP-1, it reduces JNK activation, leading to reduced phosphorylation of the JNK target c-Jun.	DISCUSS
+10	41	biochemical and structural data	evidence	Thus, our biochemical and structural data allow us to present a model for the JNK1–JIP-1–MKP7 ternary complex and provide an important insight into the assembly and function of JNK signalling modules (Supplementary Fig. 6).	DISCUSS
+78	93	JNK1–JIP-1–MKP7	complex_assembly	Thus, our biochemical and structural data allow us to present a model for the JNK1–JIP-1–MKP7 ternary complex and provide an important insight into the assembly and function of JNK signalling modules (Supplementary Fig. 6).	DISCUSS
+177	180	JNK	protein_type	Thus, our biochemical and structural data allow us to present a model for the JNK1–JIP-1–MKP7 ternary complex and provide an important insight into the assembly and function of JNK signalling modules (Supplementary Fig. 6).	DISCUSS
+13	18	human	species	The cDNAs of human MKP7 and MKP5 were kindly provided by Dr Mathijs Baens (University of Leuven) and Dr Eisuke Nishida (Kyoto University), respectively.	METHODS
+13	18	human	species	The cDNAs of human ASK1, MKK4, MKK7 and JNK1 were kindly provided by Dr Zhenguo Wu (Hong Kong University of Science and Technology).	METHODS
+4	9	human	species	The human full-length JNK1, MKK4, MKK7 and the kinase domain of ASK1 (659–951) were cloned into pGEX4T-2, pET15b and/or pET21b vectors to produce a GST- or His-tagged protein.	METHODS
+67	83	catalytic domain	structure_element	The crystal structure of unphosphorylated JNK1 in complex with the catalytic domain of MKP7 was refined to 2.4 Å resolution.	METHODS
+7	17	structures	evidence	Domain structures of ten human MKPs and the atypical VHR.	FIG
+25	30	human	species	Domain structures of ten human MKPs and the atypical VHR.	FIG
+31	35	MKPs	protein_type	Domain structures of ten human MKPs and the atypical VHR.	FIG
+53	56	VHR	protein	Domain structures of ten human MKPs and the atypical VHR.	FIG
+45	54	structure	evidence	On the basis of sequence similarity, protein structure, substrate specificity and subcellular localization, the ten members of MKP family can be divided into three groups.	FIG
+127	137	MKP family	protein_type	On the basis of sequence similarity, protein structure, substrate specificity and subcellular localization, the ten members of MKP family can be divided into three groups.	FIG
+30	34	MKP1	protein	The first subfamily comprises MKP1, MKP2, PAC1 and hVH3, which are inducible nuclear phosphatases and can dephosphorylate ERK (and JNK, p38) MAPKs.	FIG
+36	40	MKP2	protein	The first subfamily comprises MKP1, MKP2, PAC1 and hVH3, which are inducible nuclear phosphatases and can dephosphorylate ERK (and JNK, p38) MAPKs.	FIG
+42	46	PAC1	protein	The first subfamily comprises MKP1, MKP2, PAC1 and hVH3, which are inducible nuclear phosphatases and can dephosphorylate ERK (and JNK, p38) MAPKs.	FIG
+51	55	hVH3	protein	The first subfamily comprises MKP1, MKP2, PAC1 and hVH3, which are inducible nuclear phosphatases and can dephosphorylate ERK (and JNK, p38) MAPKs.	FIG
+67	76	inducible	protein_state	The first subfamily comprises MKP1, MKP2, PAC1 and hVH3, which are inducible nuclear phosphatases and can dephosphorylate ERK (and JNK, p38) MAPKs.	FIG
+77	97	nuclear phosphatases	protein_type	The first subfamily comprises MKP1, MKP2, PAC1 and hVH3, which are inducible nuclear phosphatases and can dephosphorylate ERK (and JNK, p38) MAPKs.	FIG
+122	125	ERK	protein_type	The first subfamily comprises MKP1, MKP2, PAC1 and hVH3, which are inducible nuclear phosphatases and can dephosphorylate ERK (and JNK, p38) MAPKs.	FIG
+131	134	JNK	protein_type	The first subfamily comprises MKP1, MKP2, PAC1 and hVH3, which are inducible nuclear phosphatases and can dephosphorylate ERK (and JNK, p38) MAPKs.	FIG
+136	139	p38	protein_type	The first subfamily comprises MKP1, MKP2, PAC1 and hVH3, which are inducible nuclear phosphatases and can dephosphorylate ERK (and JNK, p38) MAPKs.	FIG
+141	146	MAPKs	protein_type	The first subfamily comprises MKP1, MKP2, PAC1 and hVH3, which are inducible nuclear phosphatases and can dephosphorylate ERK (and JNK, p38) MAPKs.	FIG
+30	34	MKP3	protein	The second subfamily contains MKP3, MKP4 and MKPX, which are cytoplasmic ERK-specific MKPs.	FIG
+36	40	MKP4	protein	The second subfamily contains MKP3, MKP4 and MKPX, which are cytoplasmic ERK-specific MKPs.	FIG
+45	49	MKPX	protein	The second subfamily contains MKP3, MKP4 and MKPX, which are cytoplasmic ERK-specific MKPs.	FIG
+73	90	ERK-specific MKPs	protein_type	The second subfamily contains MKP3, MKP4 and MKPX, which are cytoplasmic ERK-specific MKPs.	FIG
+30	34	MKP5	protein	The third subfamily comprises MKP5, MKP7 and hVH5, which were located in both nucleus and cytoplasm, and selectively inactivate JNK and p38.	FIG
+36	40	MKP7	protein	The third subfamily comprises MKP5, MKP7 and hVH5, which were located in both nucleus and cytoplasm, and selectively inactivate JNK and p38.	FIG
+45	49	hVH5	protein	The third subfamily comprises MKP5, MKP7 and hVH5, which were located in both nucleus and cytoplasm, and selectively inactivate JNK and p38.	FIG
+128	131	JNK	protein_type	The third subfamily comprises MKP5, MKP7 and hVH5, which were located in both nucleus and cytoplasm, and selectively inactivate JNK and p38.	FIG
+136	139	p38	protein_type	The third subfamily comprises MKP5, MKP7 and hVH5, which were located in both nucleus and cytoplasm, and selectively inactivate JNK and p38.	FIG
+4	8	MKPs	protein_type	All MKPs contain both the CD and KBD domains, whereas VHR, an atypical MKP, only contains a highly conserved catalytic domain.	FIG
+26	28	CD	structure_element	All MKPs contain both the CD and KBD domains, whereas VHR, an atypical MKP, only contains a highly conserved catalytic domain.	FIG
+33	36	KBD	structure_element	All MKPs contain both the CD and KBD domains, whereas VHR, an atypical MKP, only contains a highly conserved catalytic domain.	FIG
+54	57	VHR	protein	All MKPs contain both the CD and KBD domains, whereas VHR, an atypical MKP, only contains a highly conserved catalytic domain.	FIG
+71	74	MKP	protein_type	All MKPs contain both the CD and KBD domains, whereas VHR, an atypical MKP, only contains a highly conserved catalytic domain.	FIG
+92	108	highly conserved	protein_state	All MKPs contain both the CD and KBD domains, whereas VHR, an atypical MKP, only contains a highly conserved catalytic domain.	FIG
+109	125	catalytic domain	structure_element	All MKPs contain both the CD and KBD domains, whereas VHR, an atypical MKP, only contains a highly conserved catalytic domain.	FIG
+19	21	CD	structure_element	In addition to the CD and KBD, MKP7 contains a unique long C-terminal region that contains NES, NLS and PEST motifs, which has no effect on the binding ability and phosphatase activity of MKP7 toward MAPKs.	FIG
+26	29	KBD	structure_element	In addition to the CD and KBD, MKP7 contains a unique long C-terminal region that contains NES, NLS and PEST motifs, which has no effect on the binding ability and phosphatase activity of MKP7 toward MAPKs.	FIG
+31	35	MKP7	protein	In addition to the CD and KBD, MKP7 contains a unique long C-terminal region that contains NES, NLS and PEST motifs, which has no effect on the binding ability and phosphatase activity of MKP7 toward MAPKs.	FIG
+59	76	C-terminal region	structure_element	In addition to the CD and KBD, MKP7 contains a unique long C-terminal region that contains NES, NLS and PEST motifs, which has no effect on the binding ability and phosphatase activity of MKP7 toward MAPKs.	FIG
+91	94	NES	structure_element	In addition to the CD and KBD, MKP7 contains a unique long C-terminal region that contains NES, NLS and PEST motifs, which has no effect on the binding ability and phosphatase activity of MKP7 toward MAPKs.	FIG
+96	99	NLS	structure_element	In addition to the CD and KBD, MKP7 contains a unique long C-terminal region that contains NES, NLS and PEST motifs, which has no effect on the binding ability and phosphatase activity of MKP7 toward MAPKs.	FIG
+104	115	PEST motifs	structure_element	In addition to the CD and KBD, MKP7 contains a unique long C-terminal region that contains NES, NLS and PEST motifs, which has no effect on the binding ability and phosphatase activity of MKP7 toward MAPKs.	FIG
+188	192	MKP7	protein	In addition to the CD and KBD, MKP7 contains a unique long C-terminal region that contains NES, NLS and PEST motifs, which has no effect on the binding ability and phosphatase activity of MKP7 toward MAPKs.	FIG
+200	205	MAPKs	protein_type	In addition to the CD and KBD, MKP7 contains a unique long C-terminal region that contains NES, NLS and PEST motifs, which has no effect on the binding ability and phosphatase activity of MKP7 toward MAPKs.	FIG
+0	3	NES	structure_element	NES, nuclear export signal; NLS, nuclear localization signal; PEST, C-terminal sequence rich in prolines, glutamates, serines and threonines.	FIG
+5	26	nuclear export signal	structure_element	NES, nuclear export signal; NLS, nuclear localization signal; PEST, C-terminal sequence rich in prolines, glutamates, serines and threonines.	FIG
+28	31	NLS	structure_element	NES, nuclear export signal; NLS, nuclear localization signal; PEST, C-terminal sequence rich in prolines, glutamates, serines and threonines.	FIG
+33	60	nuclear localization signal	structure_element	NES, nuclear export signal; NLS, nuclear localization signal; PEST, C-terminal sequence rich in prolines, glutamates, serines and threonines.	FIG
+62	66	PEST	structure_element	NES, nuclear export signal; NLS, nuclear localization signal; PEST, C-terminal sequence rich in prolines, glutamates, serines and threonines.	FIG
+68	92	C-terminal sequence rich	structure_element	NES, nuclear export signal; NLS, nuclear localization signal; PEST, C-terminal sequence rich in prolines, glutamates, serines and threonines.	FIG
+96	104	prolines	residue_name	NES, nuclear export signal; NLS, nuclear localization signal; PEST, C-terminal sequence rich in prolines, glutamates, serines and threonines.	FIG
+106	116	glutamates	residue_name	NES, nuclear export signal; NLS, nuclear localization signal; PEST, C-terminal sequence rich in prolines, glutamates, serines and threonines.	FIG
+118	125	serines	residue_name	NES, nuclear export signal; NLS, nuclear localization signal; PEST, C-terminal sequence rich in prolines, glutamates, serines and threonines.	FIG
+130	140	threonines	residue_name	NES, nuclear export signal; NLS, nuclear localization signal; PEST, C-terminal sequence rich in prolines, glutamates, serines and threonines.	FIG
+0	4	MKP7	protein	MKP7-CD is crucial for JNK1 binding and enzyme catalysis.	FIG
+5	7	CD	structure_element	MKP7-CD is crucial for JNK1 binding and enzyme catalysis.	FIG
+23	27	JNK1	protein	MKP7-CD is crucial for JNK1 binding and enzyme catalysis.	FIG
+27	32	human	species	(a) Domain organization of human MKP7 and JNK1.	FIG
+33	37	MKP7	protein	(a) Domain organization of human MKP7 and JNK1.	FIG
+42	46	JNK1	protein	(a) Domain organization of human MKP7 and JNK1.	FIG
+4	7	KBD	structure_element	The KBD and CD of MKP7 are shown in green and blue, and the N-lobe and C-lobe of JNK1 are coloured in lemon and yellow, respectively.	FIG
+12	14	CD	structure_element	The KBD and CD of MKP7 are shown in green and blue, and the N-lobe and C-lobe of JNK1 are coloured in lemon and yellow, respectively.	FIG
+18	22	MKP7	protein	The KBD and CD of MKP7 are shown in green and blue, and the N-lobe and C-lobe of JNK1 are coloured in lemon and yellow, respectively.	FIG
+60	66	N-lobe	structure_element	The KBD and CD of MKP7 are shown in green and blue, and the N-lobe and C-lobe of JNK1 are coloured in lemon and yellow, respectively.	FIG
+71	77	C-lobe	structure_element	The KBD and CD of MKP7 are shown in green and blue, and the N-lobe and C-lobe of JNK1 are coloured in lemon and yellow, respectively.	FIG
+81	85	JNK1	protein	The KBD and CD of MKP7 are shown in green and blue, and the N-lobe and C-lobe of JNK1 are coloured in lemon and yellow, respectively.	FIG
+87	112	Plots of initial velocity	evidence	The colour scheme is the same in the following figures unless indicated otherwise. (b) Plots of initial velocity of the MKP7-catalysed reaction versus phospho-JNK1 concentration.	FIG
+120	124	MKP7	protein	The colour scheme is the same in the following figures unless indicated otherwise. (b) Plots of initial velocity of the MKP7-catalysed reaction versus phospho-JNK1 concentration.	FIG
+151	158	phospho	ptm	The colour scheme is the same in the following figures unless indicated otherwise. (b) Plots of initial velocity of the MKP7-catalysed reaction versus phospho-JNK1 concentration.	FIG
+159	163	JNK1	protein	The colour scheme is the same in the following figures unless indicated otherwise. (b) Plots of initial velocity of the MKP7-catalysed reaction versus phospho-JNK1 concentration.	FIG
+36	59	Gel filtration analysis	experimental_method	The error bars represent s.e.m. (c) Gel filtration analysis for interaction of JNK1 with MKP7-CD and MKP7-KBD.	FIG
+79	83	JNK1	protein	The error bars represent s.e.m. (c) Gel filtration analysis for interaction of JNK1 with MKP7-CD and MKP7-KBD.	FIG
+89	93	MKP7	protein	The error bars represent s.e.m. (c) Gel filtration analysis for interaction of JNK1 with MKP7-CD and MKP7-KBD.	FIG
+94	96	CD	structure_element	The error bars represent s.e.m. (c) Gel filtration analysis for interaction of JNK1 with MKP7-CD and MKP7-KBD.	FIG
+101	105	MKP7	protein	The error bars represent s.e.m. (c) Gel filtration analysis for interaction of JNK1 with MKP7-CD and MKP7-KBD.	FIG
+106	109	KBD	structure_element	The error bars represent s.e.m. (c) Gel filtration analysis for interaction of JNK1 with MKP7-CD and MKP7-KBD.	FIG
+4	32	GST-mediated pull-down assay	experimental_method	(d) GST-mediated pull-down assay for interaction of JNK1 with MKP7-CD and MKP7-KBD.	FIG
+52	56	JNK1	protein	(d) GST-mediated pull-down assay for interaction of JNK1 with MKP7-CD and MKP7-KBD.	FIG
+62	66	MKP7	protein	(d) GST-mediated pull-down assay for interaction of JNK1 with MKP7-CD and MKP7-KBD.	FIG
+67	69	CD	structure_element	(d) GST-mediated pull-down assay for interaction of JNK1 with MKP7-CD and MKP7-KBD.	FIG
+74	78	MKP7	protein	(d) GST-mediated pull-down assay for interaction of JNK1 with MKP7-CD and MKP7-KBD.	FIG
+79	82	KBD	structure_element	(d) GST-mediated pull-down assay for interaction of JNK1 with MKP7-CD and MKP7-KBD.	FIG
+33	43	affinities	evidence	The top panel shows the relative affinities of MKP7-CD and MKP7-KBD to JNK1, with the affinity of MKP7-CD defined as 100%; the middle panel is the electrophoretic pattern of MKP7 and JNK1 after GST pull-down assays.	FIG
+47	51	MKP7	protein	The top panel shows the relative affinities of MKP7-CD and MKP7-KBD to JNK1, with the affinity of MKP7-CD defined as 100%; the middle panel is the electrophoretic pattern of MKP7 and JNK1 after GST pull-down assays.	FIG
+52	54	CD	structure_element	The top panel shows the relative affinities of MKP7-CD and MKP7-KBD to JNK1, with the affinity of MKP7-CD defined as 100%; the middle panel is the electrophoretic pattern of MKP7 and JNK1 after GST pull-down assays.	FIG
+59	63	MKP7	protein	The top panel shows the relative affinities of MKP7-CD and MKP7-KBD to JNK1, with the affinity of MKP7-CD defined as 100%; the middle panel is the electrophoretic pattern of MKP7 and JNK1 after GST pull-down assays.	FIG
+64	67	KBD	structure_element	The top panel shows the relative affinities of MKP7-CD and MKP7-KBD to JNK1, with the affinity of MKP7-CD defined as 100%; the middle panel is the electrophoretic pattern of MKP7 and JNK1 after GST pull-down assays.	FIG
+71	75	JNK1	protein	The top panel shows the relative affinities of MKP7-CD and MKP7-KBD to JNK1, with the affinity of MKP7-CD defined as 100%; the middle panel is the electrophoretic pattern of MKP7 and JNK1 after GST pull-down assays.	FIG
+86	94	affinity	evidence	The top panel shows the relative affinities of MKP7-CD and MKP7-KBD to JNK1, with the affinity of MKP7-CD defined as 100%; the middle panel is the electrophoretic pattern of MKP7 and JNK1 after GST pull-down assays.	FIG
+98	102	MKP7	protein	The top panel shows the relative affinities of MKP7-CD and MKP7-KBD to JNK1, with the affinity of MKP7-CD defined as 100%; the middle panel is the electrophoretic pattern of MKP7 and JNK1 after GST pull-down assays.	FIG
+103	105	CD	structure_element	The top panel shows the relative affinities of MKP7-CD and MKP7-KBD to JNK1, with the affinity of MKP7-CD defined as 100%; the middle panel is the electrophoretic pattern of MKP7 and JNK1 after GST pull-down assays.	FIG
+174	178	MKP7	protein	The top panel shows the relative affinities of MKP7-CD and MKP7-KBD to JNK1, with the affinity of MKP7-CD defined as 100%; the middle panel is the electrophoretic pattern of MKP7 and JNK1 after GST pull-down assays.	FIG
+183	187	JNK1	protein	The top panel shows the relative affinities of MKP7-CD and MKP7-KBD to JNK1, with the affinity of MKP7-CD defined as 100%; the middle panel is the electrophoretic pattern of MKP7 and JNK1 after GST pull-down assays.	FIG
+194	214	GST pull-down assays	experimental_method	The top panel shows the relative affinities of MKP7-CD and MKP7-KBD to JNK1, with the affinity of MKP7-CD defined as 100%; the middle panel is the electrophoretic pattern of MKP7 and JNK1 after GST pull-down assays.	FIG
+23	27	MKP7	protein	The protein amounts of MKP7 used are shown at the bottom.	FIG
+0	9	Structure	evidence	Structure of JNK1 in complex with MKP7-CD.	FIG
+13	17	JNK1	protein	Structure of JNK1 in complex with MKP7-CD.	FIG
+18	33	in complex with	protein_state	Structure of JNK1 in complex with MKP7-CD.	FIG
+34	38	MKP7	protein	Structure of JNK1 in complex with MKP7-CD.	FIG
+39	41	CD	structure_element	Structure of JNK1 in complex with MKP7-CD.	FIG
+22	34	JNK1–MKP7-CD	complex_assembly	(a) Ribbon diagram of JNK1–MKP7-CD complex in two views related by a 45° rotation around a vertical axis. (b) Structure of MKP7-CD with its active site highlight in cyan.	FIG
+110	119	Structure	evidence	(a) Ribbon diagram of JNK1–MKP7-CD complex in two views related by a 45° rotation around a vertical axis. (b) Structure of MKP7-CD with its active site highlight in cyan.	FIG
+123	127	MKP7	protein	(a) Ribbon diagram of JNK1–MKP7-CD complex in two views related by a 45° rotation around a vertical axis. (b) Structure of MKP7-CD with its active site highlight in cyan.	FIG
+128	130	CD	structure_element	(a) Ribbon diagram of JNK1–MKP7-CD complex in two views related by a 45° rotation around a vertical axis. (b) Structure of MKP7-CD with its active site highlight in cyan.	FIG
+140	151	active site	site	(a) Ribbon diagram of JNK1–MKP7-CD complex in two views related by a 45° rotation around a vertical axis. (b) Structure of MKP7-CD with its active site highlight in cyan.	FIG
+4	19	2Fo−Fc omit map	evidence	The 2Fo−Fc omit map (contoured at 1.5σ) for the P-loop of MKP7-CD is shown at inset of b. (c) Structure of VHR with its active site highlighted in marine blue. (d) Close-up view of the JNK1–MKP7 interface showing interacting amino acids of JNK1 (orange) and MKP7-CD (cyan).	FIG
+48	54	P-loop	structure_element	The 2Fo−Fc omit map (contoured at 1.5σ) for the P-loop of MKP7-CD is shown at inset of b. (c) Structure of VHR with its active site highlighted in marine blue. (d) Close-up view of the JNK1–MKP7 interface showing interacting amino acids of JNK1 (orange) and MKP7-CD (cyan).	FIG
+58	62	MKP7	protein	The 2Fo−Fc omit map (contoured at 1.5σ) for the P-loop of MKP7-CD is shown at inset of b. (c) Structure of VHR with its active site highlighted in marine blue. (d) Close-up view of the JNK1–MKP7 interface showing interacting amino acids of JNK1 (orange) and MKP7-CD (cyan).	FIG
+63	65	CD	structure_element	The 2Fo−Fc omit map (contoured at 1.5σ) for the P-loop of MKP7-CD is shown at inset of b. (c) Structure of VHR with its active site highlighted in marine blue. (d) Close-up view of the JNK1–MKP7 interface showing interacting amino acids of JNK1 (orange) and MKP7-CD (cyan).	FIG
+94	103	Structure	evidence	The 2Fo−Fc omit map (contoured at 1.5σ) for the P-loop of MKP7-CD is shown at inset of b. (c) Structure of VHR with its active site highlighted in marine blue. (d) Close-up view of the JNK1–MKP7 interface showing interacting amino acids of JNK1 (orange) and MKP7-CD (cyan).	FIG
+107	110	VHR	protein	The 2Fo−Fc omit map (contoured at 1.5σ) for the P-loop of MKP7-CD is shown at inset of b. (c) Structure of VHR with its active site highlighted in marine blue. (d) Close-up view of the JNK1–MKP7 interface showing interacting amino acids of JNK1 (orange) and MKP7-CD (cyan).	FIG
+120	131	active site	site	The 2Fo−Fc omit map (contoured at 1.5σ) for the P-loop of MKP7-CD is shown at inset of b. (c) Structure of VHR with its active site highlighted in marine blue. (d) Close-up view of the JNK1–MKP7 interface showing interacting amino acids of JNK1 (orange) and MKP7-CD (cyan).	FIG
+185	204	JNK1–MKP7 interface	site	The 2Fo−Fc omit map (contoured at 1.5σ) for the P-loop of MKP7-CD is shown at inset of b. (c) Structure of VHR with its active site highlighted in marine blue. (d) Close-up view of the JNK1–MKP7 interface showing interacting amino acids of JNK1 (orange) and MKP7-CD (cyan).	FIG
+240	244	JNK1	protein	The 2Fo−Fc omit map (contoured at 1.5σ) for the P-loop of MKP7-CD is shown at inset of b. (c) Structure of VHR with its active site highlighted in marine blue. (d) Close-up view of the JNK1–MKP7 interface showing interacting amino acids of JNK1 (orange) and MKP7-CD (cyan).	FIG
+258	262	MKP7	protein	The 2Fo−Fc omit map (contoured at 1.5σ) for the P-loop of MKP7-CD is shown at inset of b. (c) Structure of VHR with its active site highlighted in marine blue. (d) Close-up view of the JNK1–MKP7 interface showing interacting amino acids of JNK1 (orange) and MKP7-CD (cyan).	FIG
+263	265	CD	structure_element	The 2Fo−Fc omit map (contoured at 1.5σ) for the P-loop of MKP7-CD is shown at inset of b. (c) Structure of VHR with its active site highlighted in marine blue. (d) Close-up view of the JNK1–MKP7 interface showing interacting amino acids of JNK1 (orange) and MKP7-CD (cyan).	FIG
+4	8	JNK1	protein	The JNK1 is shown in surface representation coloured according to electrostatic potential (positive, blue; negative, red).	FIG
+4	24	Interaction networks	site	(e) Interaction networks mainly involving helices α4 and α5 from MKP7-CD, and αG and α2L14 of JNK1.	FIG
+42	49	helices	structure_element	(e) Interaction networks mainly involving helices α4 and α5 from MKP7-CD, and αG and α2L14 of JNK1.	FIG
+50	52	α4	structure_element	(e) Interaction networks mainly involving helices α4 and α5 from MKP7-CD, and αG and α2L14 of JNK1.	FIG
+57	59	α5	structure_element	(e) Interaction networks mainly involving helices α4 and α5 from MKP7-CD, and αG and α2L14 of JNK1.	FIG
+65	69	MKP7	protein	(e) Interaction networks mainly involving helices α4 and α5 from MKP7-CD, and αG and α2L14 of JNK1.	FIG
+70	72	CD	structure_element	(e) Interaction networks mainly involving helices α4 and α5 from MKP7-CD, and αG and α2L14 of JNK1.	FIG
+78	80	αG	structure_element	(e) Interaction networks mainly involving helices α4 and α5 from MKP7-CD, and αG and α2L14 of JNK1.	FIG
+85	90	α2L14	structure_element	(e) Interaction networks mainly involving helices α4 and α5 from MKP7-CD, and αG and α2L14 of JNK1.	FIG
+94	98	JNK1	protein	(e) Interaction networks mainly involving helices α4 and α5 from MKP7-CD, and αG and α2L14 of JNK1.	FIG
+0	4	MKP7	protein	MKP7-CD is shown in surface representation coloured according to electrostatic potential (positive, blue; negative, red).	FIG
+5	7	CD	structure_element	MKP7-CD is shown in surface representation coloured according to electrostatic potential (positive, blue; negative, red).	FIG
+28	46	polar interactions	bond_interaction	Blue dashed lines represent polar interactions.	FIG
+28	46	polar interactions	bond_interaction	Blue dashed lines represent polar interactions.	FIG
+8	23	2Fo−Fc omit map	evidence	(f) The 2Fo−Fc omit map (contoured at 1.5σ) clearly shows electron density for the 285FNFL288 segment of MKP7-CD.	FIG
+58	74	electron density	evidence	(f) The 2Fo−Fc omit map (contoured at 1.5σ) clearly shows electron density for the 285FNFL288 segment of MKP7-CD.	FIG
+83	101	285FNFL288 segment	structure_element	(f) The 2Fo−Fc omit map (contoured at 1.5σ) clearly shows electron density for the 285FNFL288 segment of MKP7-CD.	FIG
+105	109	MKP7	protein	(f) The 2Fo−Fc omit map (contoured at 1.5σ) clearly shows electron density for the 285FNFL288 segment of MKP7-CD.	FIG
+110	112	CD	structure_element	(f) The 2Fo−Fc omit map (contoured at 1.5σ) clearly shows electron density for the 285FNFL288 segment of MKP7-CD.	FIG
+0	19	Mutational analysis	experimental_method	Mutational analysis on interactions between MKP7-CD and JNK1.	FIG
+44	48	MKP7	protein	Mutational analysis on interactions between MKP7-CD and JNK1.	FIG
+49	51	CD	structure_element	Mutational analysis on interactions between MKP7-CD and JNK1.	FIG
+56	60	JNK1	protein	Mutational analysis on interactions between MKP7-CD and JNK1.	FIG
+28	32	MKP7	protein	(a) Effects of mutations in MKP7-CD on the JNK1 dephosphorylation (mean±s.e.m., n=3).	FIG
+33	35	CD	structure_element	(a) Effects of mutations in MKP7-CD on the JNK1 dephosphorylation (mean±s.e.m., n=3).	FIG
+43	47	JNK1	protein	(a) Effects of mutations in MKP7-CD on the JNK1 dephosphorylation (mean±s.e.m., n=3).	FIG
+48	65	dephosphorylation	ptm	(a) Effects of mutations in MKP7-CD on the JNK1 dephosphorylation (mean±s.e.m., n=3).	FIG
+21	57	hydrophobic and hydrophilic contacts	bond_interaction	Residues involved in hydrophobic and hydrophilic contacts are coloured in red and blue, respectively. (b) Gel filtration analysis for interaction of JNK1 with MKP7-CD mutant F285D.	FIG
+106	129	Gel filtration analysis	experimental_method	Residues involved in hydrophobic and hydrophilic contacts are coloured in red and blue, respectively. (b) Gel filtration analysis for interaction of JNK1 with MKP7-CD mutant F285D.	FIG
+149	153	JNK1	protein	Residues involved in hydrophobic and hydrophilic contacts are coloured in red and blue, respectively. (b) Gel filtration analysis for interaction of JNK1 with MKP7-CD mutant F285D.	FIG
+159	163	MKP7	protein	Residues involved in hydrophobic and hydrophilic contacts are coloured in red and blue, respectively. (b) Gel filtration analysis for interaction of JNK1 with MKP7-CD mutant F285D.	FIG
+164	166	CD	structure_element	Residues involved in hydrophobic and hydrophilic contacts are coloured in red and blue, respectively. (b) Gel filtration analysis for interaction of JNK1 with MKP7-CD mutant F285D.	FIG
+167	173	mutant	protein_state	Residues involved in hydrophobic and hydrophilic contacts are coloured in red and blue, respectively. (b) Gel filtration analysis for interaction of JNK1 with MKP7-CD mutant F285D.	FIG
+174	179	F285D	mutant	Residues involved in hydrophobic and hydrophilic contacts are coloured in red and blue, respectively. (b) Gel filtration analysis for interaction of JNK1 with MKP7-CD mutant F285D.	FIG
+0	6	Mutant	protein_state	Mutant F285D and JNK1 were eluted as monomers, with the molecular masses of ∼17 and 44 kDa, respectively.	FIG
+7	12	F285D	mutant	Mutant F285D and JNK1 were eluted as monomers, with the molecular masses of ∼17 and 44 kDa, respectively.	FIG
+17	21	JNK1	protein	Mutant F285D and JNK1 were eluted as monomers, with the molecular masses of ∼17 and 44 kDa, respectively.	FIG
+37	45	monomers	oligomeric_state	Mutant F285D and JNK1 were eluted as monomers, with the molecular masses of ∼17 and 44 kDa, respectively.	FIG
+28	37	wild-type	protein_state	However, in contrast to the wild-type MKP7-CD, mutant F285D did not co-migrate with JNK1.	FIG
+38	42	MKP7	protein	However, in contrast to the wild-type MKP7-CD, mutant F285D did not co-migrate with JNK1.	FIG
+43	45	CD	structure_element	However, in contrast to the wild-type MKP7-CD, mutant F285D did not co-migrate with JNK1.	FIG
+47	53	mutant	protein_state	However, in contrast to the wild-type MKP7-CD, mutant F285D did not co-migrate with JNK1.	FIG
+54	59	F285D	mutant	However, in contrast to the wild-type MKP7-CD, mutant F285D did not co-migrate with JNK1.	FIG
+84	88	JNK1	protein	However, in contrast to the wild-type MKP7-CD, mutant F285D did not co-migrate with JNK1.	FIG
+4	20	Pull-down assays	experimental_method	(c) Pull-down assays of MKP7-CD by GST-tagged JNK1 mutants.	FIG
+24	28	MKP7	protein	(c) Pull-down assays of MKP7-CD by GST-tagged JNK1 mutants.	FIG
+29	31	CD	structure_element	(c) Pull-down assays of MKP7-CD by GST-tagged JNK1 mutants.	FIG
+35	45	GST-tagged	protein_state	(c) Pull-down assays of MKP7-CD by GST-tagged JNK1 mutants.	FIG
+46	50	JNK1	protein	(c) Pull-down assays of MKP7-CD by GST-tagged JNK1 mutants.	FIG
+51	58	mutants	protein_state	(c) Pull-down assays of MKP7-CD by GST-tagged JNK1 mutants.	FIG
+33	43	affinities	evidence	The top panel shows the relative affinities of MKP7-CD to JNK1 mutants, with the affinity of wild-type JNK1 defined as 100%, the middle panel is the electrophoretic pattern of MKP7-CD and JNK1 mutants after GST pull-down assays.	FIG
+47	51	MKP7	protein	The top panel shows the relative affinities of MKP7-CD to JNK1 mutants, with the affinity of wild-type JNK1 defined as 100%, the middle panel is the electrophoretic pattern of MKP7-CD and JNK1 mutants after GST pull-down assays.	FIG
+52	54	CD	structure_element	The top panel shows the relative affinities of MKP7-CD to JNK1 mutants, with the affinity of wild-type JNK1 defined as 100%, the middle panel is the electrophoretic pattern of MKP7-CD and JNK1 mutants after GST pull-down assays.	FIG
+58	62	JNK1	protein	The top panel shows the relative affinities of MKP7-CD to JNK1 mutants, with the affinity of wild-type JNK1 defined as 100%, the middle panel is the electrophoretic pattern of MKP7-CD and JNK1 mutants after GST pull-down assays.	FIG
+63	70	mutants	protein_state	The top panel shows the relative affinities of MKP7-CD to JNK1 mutants, with the affinity of wild-type JNK1 defined as 100%, the middle panel is the electrophoretic pattern of MKP7-CD and JNK1 mutants after GST pull-down assays.	FIG
+81	89	affinity	evidence	The top panel shows the relative affinities of MKP7-CD to JNK1 mutants, with the affinity of wild-type JNK1 defined as 100%, the middle panel is the electrophoretic pattern of MKP7-CD and JNK1 mutants after GST pull-down assays.	FIG
+93	102	wild-type	protein_state	The top panel shows the relative affinities of MKP7-CD to JNK1 mutants, with the affinity of wild-type JNK1 defined as 100%, the middle panel is the electrophoretic pattern of MKP7-CD and JNK1 mutants after GST pull-down assays.	FIG
+103	107	JNK1	protein	The top panel shows the relative affinities of MKP7-CD to JNK1 mutants, with the affinity of wild-type JNK1 defined as 100%, the middle panel is the electrophoretic pattern of MKP7-CD and JNK1 mutants after GST pull-down assays.	FIG
+176	180	MKP7	protein	The top panel shows the relative affinities of MKP7-CD to JNK1 mutants, with the affinity of wild-type JNK1 defined as 100%, the middle panel is the electrophoretic pattern of MKP7-CD and JNK1 mutants after GST pull-down assays.	FIG
+181	183	CD	structure_element	The top panel shows the relative affinities of MKP7-CD to JNK1 mutants, with the affinity of wild-type JNK1 defined as 100%, the middle panel is the electrophoretic pattern of MKP7-CD and JNK1 mutants after GST pull-down assays.	FIG
+188	192	JNK1	protein	The top panel shows the relative affinities of MKP7-CD to JNK1 mutants, with the affinity of wild-type JNK1 defined as 100%, the middle panel is the electrophoretic pattern of MKP7-CD and JNK1 mutants after GST pull-down assays.	FIG
+193	200	mutants	protein_state	The top panel shows the relative affinities of MKP7-CD to JNK1 mutants, with the affinity of wild-type JNK1 defined as 100%, the middle panel is the electrophoretic pattern of MKP7-CD and JNK1 mutants after GST pull-down assays.	FIG
+207	227	GST pull-down assays	experimental_method	The top panel shows the relative affinities of MKP7-CD to JNK1 mutants, with the affinity of wild-type JNK1 defined as 100%, the middle panel is the electrophoretic pattern of MKP7-CD and JNK1 mutants after GST pull-down assays.	FIG
+23	27	MKP7	protein	The protein amounts of MKP7-CD used are shown at the bottom. (d) Circular dichroism spectra for MKP7-CD wild type and mutants.	FIG
+28	30	CD	structure_element	The protein amounts of MKP7-CD used are shown at the bottom. (d) Circular dichroism spectra for MKP7-CD wild type and mutants.	FIG
+65	83	Circular dichroism	experimental_method	The protein amounts of MKP7-CD used are shown at the bottom. (d) Circular dichroism spectra for MKP7-CD wild type and mutants.	FIG
+84	91	spectra	evidence	The protein amounts of MKP7-CD used are shown at the bottom. (d) Circular dichroism spectra for MKP7-CD wild type and mutants.	FIG
+96	100	MKP7	protein	The protein amounts of MKP7-CD used are shown at the bottom. (d) Circular dichroism spectra for MKP7-CD wild type and mutants.	FIG
+101	103	CD	structure_element	The protein amounts of MKP7-CD used are shown at the bottom. (d) Circular dichroism spectra for MKP7-CD wild type and mutants.	FIG
+104	113	wild type	protein_state	The protein amounts of MKP7-CD used are shown at the bottom. (d) Circular dichroism spectra for MKP7-CD wild type and mutants.	FIG
+118	125	mutants	protein_state	The protein amounts of MKP7-CD used are shown at the bottom. (d) Circular dichroism spectra for MKP7-CD wild type and mutants.	FIG
+48	66	Circular dichroism	experimental_method	Measurements were averaged for three scans. (e) Circular dichroism spectra for JNK1 wild type and mutants.	FIG
+67	74	spectra	evidence	Measurements were averaged for three scans. (e) Circular dichroism spectra for JNK1 wild type and mutants.	FIG
+79	83	JNK1	protein	Measurements were averaged for three scans. (e) Circular dichroism spectra for JNK1 wild type and mutants.	FIG
+84	93	wild type	protein_state	Measurements were averaged for three scans. (e) Circular dichroism spectra for JNK1 wild type and mutants.	FIG
+98	105	mutants	protein_state	Measurements were averaged for three scans. (e) Circular dichroism spectra for JNK1 wild type and mutants.	FIG
+15	24	mutations	experimental_method	(f) Effects of mutations in MKP7-CD on the pNPP hydrolysis reaction (mean±s.e.m., n=3).	FIG
+28	32	MKP7	protein	(f) Effects of mutations in MKP7-CD on the pNPP hydrolysis reaction (mean±s.e.m., n=3).	FIG
+33	35	CD	structure_element	(f) Effects of mutations in MKP7-CD on the pNPP hydrolysis reaction (mean±s.e.m., n=3).	FIG
+43	47	pNPP	chemical	(f) Effects of mutations in MKP7-CD on the pNPP hydrolysis reaction (mean±s.e.m., n=3).	FIG
+14	22	CDK2-KAP	complex_assembly	Comparison of CDK2-KAP and JNK1–MKP7-CD.	FIG
+27	39	JNK1–MKP7-CD	complex_assembly	Comparison of CDK2-KAP and JNK1–MKP7-CD.	FIG
+4	17	Superposition	experimental_method	(a) Superposition of the complex structures of CDK2-KAP (PDB 1FQ1) and JNK1–MKP7-CD.	FIG
+33	43	structures	evidence	(a) Superposition of the complex structures of CDK2-KAP (PDB 1FQ1) and JNK1–MKP7-CD.	FIG
+47	55	CDK2-KAP	complex_assembly	(a) Superposition of the complex structures of CDK2-KAP (PDB 1FQ1) and JNK1–MKP7-CD.	FIG
+71	83	JNK1–MKP7-CD	complex_assembly	(a) Superposition of the complex structures of CDK2-KAP (PDB 1FQ1) and JNK1–MKP7-CD.	FIG
+4	10	N-lobe	structure_element	The N-lobe and C-lobe of CDK2 are coloured in grey and pink, respectively, and KAP is coloured in green.	FIG
+15	21	C-lobe	structure_element	The N-lobe and C-lobe of CDK2 are coloured in grey and pink, respectively, and KAP is coloured in green.	FIG
+25	29	CDK2	protein	The N-lobe and C-lobe of CDK2 are coloured in grey and pink, respectively, and KAP is coloured in green.	FIG
+79	82	KAP	protein	The N-lobe and C-lobe of CDK2 are coloured in grey and pink, respectively, and KAP is coloured in green.	FIG
+75	90	contact regions	site	The interactions between these two proteins consist of three discontinuous contact regions, centred at the multiple hydrogen bonds between the pThr160 of CDK2 and the active site of KAP (region I).	FIG
+116	130	hydrogen bonds	bond_interaction	The interactions between these two proteins consist of three discontinuous contact regions, centred at the multiple hydrogen bonds between the pThr160 of CDK2 and the active site of KAP (region I).	FIG
+143	150	pThr160	ptm	The interactions between these two proteins consist of three discontinuous contact regions, centred at the multiple hydrogen bonds between the pThr160 of CDK2 and the active site of KAP (region I).	FIG
+154	158	CDK2	protein	The interactions between these two proteins consist of three discontinuous contact regions, centred at the multiple hydrogen bonds between the pThr160 of CDK2 and the active site of KAP (region I).	FIG
+167	178	active site	site	The interactions between these two proteins consist of three discontinuous contact regions, centred at the multiple hydrogen bonds between the pThr160 of CDK2 and the active site of KAP (region I).	FIG
+182	185	KAP	protein	The interactions between these two proteins consist of three discontinuous contact regions, centred at the multiple hydrogen bonds between the pThr160 of CDK2 and the active site of KAP (region I).	FIG
+187	195	region I	structure_element	The interactions between these two proteins consist of three discontinuous contact regions, centred at the multiple hydrogen bonds between the pThr160 of CDK2 and the active site of KAP (region I).	FIG
+34	38	CDK2	protein	Interestingly, the recognition of CDK2 by KAP is augmented by a similar interface as that observed in the complex of JNK1 and MKP7-CD (region II).	FIG
+42	45	KAP	protein	Interestingly, the recognition of CDK2 by KAP is augmented by a similar interface as that observed in the complex of JNK1 and MKP7-CD (region II).	FIG
+72	81	interface	site	Interestingly, the recognition of CDK2 by KAP is augmented by a similar interface as that observed in the complex of JNK1 and MKP7-CD (region II).	FIG
+117	121	JNK1	protein	Interestingly, the recognition of CDK2 by KAP is augmented by a similar interface as that observed in the complex of JNK1 and MKP7-CD (region II).	FIG
+126	130	MKP7	protein	Interestingly, the recognition of CDK2 by KAP is augmented by a similar interface as that observed in the complex of JNK1 and MKP7-CD (region II).	FIG
+131	133	CD	structure_element	Interestingly, the recognition of CDK2 by KAP is augmented by a similar interface as that observed in the complex of JNK1 and MKP7-CD (region II).	FIG
+135	144	region II	structure_element	Interestingly, the recognition of CDK2 by KAP is augmented by a similar interface as that observed in the complex of JNK1 and MKP7-CD (region II).	FIG
+33	52	auxiliary region II	structure_element	(b) Interactions networks at the auxiliary region II mainly involving helix α7 from KAP and the αG helix and following L14 loop of CDK2.	FIG
+70	75	helix	structure_element	(b) Interactions networks at the auxiliary region II mainly involving helix α7 from KAP and the αG helix and following L14 loop of CDK2.	FIG
+76	78	α7	structure_element	(b) Interactions networks at the auxiliary region II mainly involving helix α7 from KAP and the αG helix and following L14 loop of CDK2.	FIG
+84	87	KAP	protein	(b) Interactions networks at the auxiliary region II mainly involving helix α7 from KAP and the αG helix and following L14 loop of CDK2.	FIG
+96	104	αG helix	structure_element	(b) Interactions networks at the auxiliary region II mainly involving helix α7 from KAP and the αG helix and following L14 loop of CDK2.	FIG
+119	127	L14 loop	structure_element	(b) Interactions networks at the auxiliary region II mainly involving helix α7 from KAP and the αG helix and following L14 loop of CDK2.	FIG
+131	135	CDK2	protein	(b) Interactions networks at the auxiliary region II mainly involving helix α7 from KAP and the αG helix and following L14 loop of CDK2.	FIG
+4	8	CDK2	protein	The CDK2 is shown in surface representation coloured according to the electrostatic potential (positive, blue; negative, red).	FIG
+12	15	KAP	protein	Residues of KAP and CDK2 are highlighted as green and red sticks, respectively.	FIG
+20	24	CDK2	protein	Residues of KAP and CDK2 are highlighted as green and red sticks, respectively.	FIG
+81	86	helix	structure_element	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+87	89	α6	structure_element	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+93	96	KAP	protein	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+115	120	helix	structure_element	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+121	123	α4	structure_element	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+127	131	MKP7	protein	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+132	134	CD	structure_element	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+185	191	stable	protein_state	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+192	203	heterodimer	oligomeric_state	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+207	211	CDK2	protein	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+216	219	KAP	protein	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+225	243	Sequence alignment	experimental_method	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+251	274	JNK-interacting regions	site	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+278	282	MKPs	protein_type	One remarkable difference between these two kinase-phosphatase complexes is that helix α6 of KAP (corresponding to helix α4 of MKP7-CD) plays little, if any, role in the formation of a stable heterodimer of CDK2 and KAP. (c) Sequence alignment of the JNK-interacting regions on MKPs.	FIG
+12	16	MKP7	protein	Residues of MKP7-CD involved in JNK1 recognition are indicated by cyan asterisks, and the conserved FXF-motif is highlighted in cyan.	FIG
+17	19	CD	structure_element	Residues of MKP7-CD involved in JNK1 recognition are indicated by cyan asterisks, and the conserved FXF-motif is highlighted in cyan.	FIG
+32	36	JNK1	protein	Residues of MKP7-CD involved in JNK1 recognition are indicated by cyan asterisks, and the conserved FXF-motif is highlighted in cyan.	FIG
+90	99	conserved	protein_state	Residues of MKP7-CD involved in JNK1 recognition are indicated by cyan asterisks, and the conserved FXF-motif is highlighted in cyan.	FIG
+100	109	FXF-motif	structure_element	Residues of MKP7-CD involved in JNK1 recognition are indicated by cyan asterisks, and the conserved FXF-motif is highlighted in cyan.	FIG
+39	43	MKP7	protein	The secondary structure assignments of MKP7-CD and KAP are shown above and below each sequence.	FIG
+44	46	CD	structure_element	The secondary structure assignments of MKP7-CD and KAP are shown above and below each sequence.	FIG
+51	54	KAP	protein	The secondary structure assignments of MKP7-CD and KAP are shown above and below each sequence.	FIG
+4	22	Sequence alignment	experimental_method	(d) Sequence alignment of the F-site regions on MAPKs.	FIG
+30	44	F-site regions	structure_element	(d) Sequence alignment of the F-site regions on MAPKs.	FIG
+48	53	MAPKs	protein_type	(d) Sequence alignment of the F-site regions on MAPKs.	FIG
+12	16	JNK1	protein	Residues of JNK1 involved in recognition of MKP7 are indicated by orange asterisks, and those forming the F-site are highlighted in yellow.	FIG
+44	48	MKP7	protein	Residues of JNK1 involved in recognition of MKP7 are indicated by orange asterisks, and those forming the F-site are highlighted in yellow.	FIG
+106	112	F-site	site	Residues of JNK1 involved in recognition of MKP7 are indicated by orange asterisks, and those forming the F-site are highlighted in yellow.	FIG
+0	9	FXF-motif	structure_element	FXF-motif is critical for controlling the phosphorylation of JNK and ultraviolet-induced apoptosis.	FIG
+42	57	phosphorylation	ptm	FXF-motif is critical for controlling the phosphorylation of JNK and ultraviolet-induced apoptosis.	FIG
+61	64	JNK	protein_type	FXF-motif is critical for controlling the phosphorylation of JNK and ultraviolet-induced apoptosis.	FIG
+6	15	FXF-motif	structure_element	(a–c) FXF-motif is essential for the dephosphorylation of JNK by MKP7.	FIG
+58	61	JNK	protein_type	(a–c) FXF-motif is essential for the dephosphorylation of JNK by MKP7.	FIG
+65	69	MKP7	protein	(a–c) FXF-motif is essential for the dephosphorylation of JNK by MKP7.	FIG
+33	45	lentiviruses	taxonomy_domain	HEK293T cells were infected with lentiviruses expressing MKP7 and its mutants (1.0 μg).	FIG
+57	61	MKP7	protein	HEK293T cells were infected with lentiviruses expressing MKP7 and its mutants (1.0 μg).	FIG
+70	77	mutants	protein_state	HEK293T cells were infected with lentiviruses expressing MKP7 and its mutants (1.0 μg).	FIG
+71	80	etoposide	chemical	After 36 h infection, cells were untreated in a, stimulated with 30 μM etoposide for 3 h in b or irradiated with 25 J m−2 ultraviolet light at 30 min before lysis in c. Whole-cell extracts were then immunoblotted with antibody indicated.	FIG
+34	48	phosphorylated	protein_state	Shown is a typical immunoblot for phosphorylated JNK from three independent experiments.	FIG
+49	52	JNK	protein_type	Shown is a typical immunoblot for phosphorylated JNK from three independent experiments.	FIG
+4	10	F-site	site	(d) F-site is required for JNK1 to interact with MKP7.	FIG
+27	31	JNK1	protein	(d) F-site is required for JNK1 to interact with MKP7.	FIG
+49	53	MKP7	protein	(d) F-site is required for JNK1 to interact with MKP7.	FIG
+19	33	co-transfected	experimental_method	HEK293T cells were co-transfected with MKP7 full-length (1.0 μg) and JNK1 (wild type or mutants as indicated, 1.0 μg).	FIG
+39	43	MKP7	protein	HEK293T cells were co-transfected with MKP7 full-length (1.0 μg) and JNK1 (wild type or mutants as indicated, 1.0 μg).	FIG
+44	55	full-length	protein_state	HEK293T cells were co-transfected with MKP7 full-length (1.0 μg) and JNK1 (wild type or mutants as indicated, 1.0 μg).	FIG
+69	73	JNK1	protein	HEK293T cells were co-transfected with MKP7 full-length (1.0 μg) and JNK1 (wild type or mutants as indicated, 1.0 μg).	FIG
+75	84	wild type	protein_state	HEK293T cells were co-transfected with MKP7 full-length (1.0 μg) and JNK1 (wild type or mutants as indicated, 1.0 μg).	FIG
+88	95	mutants	protein_state	HEK293T cells were co-transfected with MKP7 full-length (1.0 μg) and JNK1 (wild type or mutants as indicated, 1.0 μg).	FIG
+30	48	immunoprecipitated	experimental_method	Whole-cell extracts were then immunoprecipitated with antibody against Myc for MKP7; immunobloting was carried out with antibodies indicated.	FIG
+79	83	MKP7	protein	Whole-cell extracts were then immunoprecipitated with antibody against Myc for MKP7; immunobloting was carried out with antibodies indicated.	FIG
+0	2	IP	experimental_method	IP, immunoprecipitation; TCL, total cell lysate.	FIG
+4	23	immunoprecipitation	experimental_method	IP, immunoprecipitation; TCL, total cell lysate.	FIG
+14	18	MKP7	protein	(e) Effect of MKP7 (wild type or mutants) expression on ultraviolet-induced apoptosis.	FIG
+20	29	wild type	protein_state	(e) Effect of MKP7 (wild type or mutants) expression on ultraviolet-induced apoptosis.	FIG
+33	40	mutants	protein_state	(e) Effect of MKP7 (wild type or mutants) expression on ultraviolet-induced apoptosis.	FIG
+30	42	lentiviruses	taxonomy_domain	HeLa cells were infected with lentiviruses expressing MKP7 full-length and its mutants.	FIG
+54	58	MKP7	protein	HeLa cells were infected with lentiviruses expressing MKP7 full-length and its mutants.	FIG
+59	70	full-length	protein_state	HeLa cells were infected with lentiviruses expressing MKP7 full-length and its mutants.	FIG
+79	86	mutants	protein_state	HeLa cells were infected with lentiviruses expressing MKP7 full-length and its mutants.	FIG
+29	43	flow cytometry	experimental_method	Cells were then subjected to flow cytometry analysis.	FIG
+35	48	Annexin-V-APC	chemical	Apoptotic cells were determined by Annexin-V-APC/PI staining.	FIG
+49	51	PI	chemical	Apoptotic cells were determined by Annexin-V-APC/PI staining.	FIG
+18	27	Annexin-V	chemical	The results using Annexin-V stain for membrane phosphatidylserine eversion, combined with propidium iodide (PI) uptake to evaluate cells whose membranes had been compromised.	FIG
+90	106	propidium iodide	chemical	The results using Annexin-V stain for membrane phosphatidylserine eversion, combined with propidium iodide (PI) uptake to evaluate cells whose membranes had been compromised.	FIG
+108	110	PI	chemical	The results using Annexin-V stain for membrane phosphatidylserine eversion, combined with propidium iodide (PI) uptake to evaluate cells whose membranes had been compromised.	FIG
+19	28	Annexin-V	chemical	Staining with both Annexin-V and PI indicate apoptosis (upper right quadrant).	FIG
+33	35	PI	chemical	Staining with both Annexin-V and PI indicate apoptosis (upper right quadrant).	FIG
+64	66	*P	evidence	(f) Statistical analysis of apoptotic cells (mean±s.e.m., n=3), *P<0.05, ***P<0.001 (ANOVA followed by Tukey's test).	FIG
+73	77	***P	evidence	(f) Statistical analysis of apoptotic cells (mean±s.e.m., n=3), *P<0.05, ***P<0.001 (ANOVA followed by Tukey's test).	FIG
+85	90	ANOVA	experimental_method	(f) Statistical analysis of apoptotic cells (mean±s.e.m., n=3), *P<0.05, ***P<0.001 (ANOVA followed by Tukey's test).	FIG
+103	115	Tukey's test	experimental_method	(f) Statistical analysis of apoptotic cells (mean±s.e.m., n=3), *P<0.05, ***P<0.001 (ANOVA followed by Tukey's test).	FIG
+0	4	MKP5	protein	MKP5-CD is crucial for JNK1 binding and enzyme catalysis.	FIG
+5	7	CD	structure_element	MKP5-CD is crucial for JNK1 binding and enzyme catalysis.	FIG
+23	27	JNK1	protein	MKP5-CD is crucial for JNK1 binding and enzyme catalysis.	FIG
+27	32	human	species	(a) Domain organization of human MKP5.	FIG
+33	37	MKP5	protein	(a) Domain organization of human MKP5.	FIG
+4	7	KBD	structure_element	The KBD and CD of MKP5 are shown in brown and grey, respectively. (b) Plots of initial velocity of the MKP5-catalysed reaction versus phospho-JNK1 concentration.	FIG
+12	14	CD	structure_element	The KBD and CD of MKP5 are shown in brown and grey, respectively. (b) Plots of initial velocity of the MKP5-catalysed reaction versus phospho-JNK1 concentration.	FIG
+18	22	MKP5	protein	The KBD and CD of MKP5 are shown in brown and grey, respectively. (b) Plots of initial velocity of the MKP5-catalysed reaction versus phospho-JNK1 concentration.	FIG
+70	95	Plots of initial velocity	evidence	The KBD and CD of MKP5 are shown in brown and grey, respectively. (b) Plots of initial velocity of the MKP5-catalysed reaction versus phospho-JNK1 concentration.	FIG
+103	107	MKP5	protein	The KBD and CD of MKP5 are shown in brown and grey, respectively. (b) Plots of initial velocity of the MKP5-catalysed reaction versus phospho-JNK1 concentration.	FIG
+134	141	phospho	protein_state	The KBD and CD of MKP5 are shown in brown and grey, respectively. (b) Plots of initial velocity of the MKP5-catalysed reaction versus phospho-JNK1 concentration.	FIG
+142	146	JNK1	protein	The KBD and CD of MKP5 are shown in brown and grey, respectively. (b) Plots of initial velocity of the MKP5-catalysed reaction versus phospho-JNK1 concentration.	FIG
+89	91	Km	evidence	The solid lines are best-fitting results according to the Michaelis–Menten equation with Km and kcat values indicated.	FIG
+96	100	kcat	evidence	The solid lines are best-fitting results according to the Michaelis–Menten equation with Km and kcat values indicated.	FIG
+36	57	Structural comparison	experimental_method	The error bars represent s.e.m. (c) Structural comparison of the JNK-interacting residues on MKP5-CD (PDB 1ZZW) and MKP7-CD.	FIG
+65	89	JNK-interacting residues	site	The error bars represent s.e.m. (c) Structural comparison of the JNK-interacting residues on MKP5-CD (PDB 1ZZW) and MKP7-CD.	FIG
+93	97	MKP5	protein	The error bars represent s.e.m. (c) Structural comparison of the JNK-interacting residues on MKP5-CD (PDB 1ZZW) and MKP7-CD.	FIG
+98	100	CD	structure_element	The error bars represent s.e.m. (c) Structural comparison of the JNK-interacting residues on MKP5-CD (PDB 1ZZW) and MKP7-CD.	FIG
+116	120	MKP7	protein	The error bars represent s.e.m. (c) Structural comparison of the JNK-interacting residues on MKP5-CD (PDB 1ZZW) and MKP7-CD.	FIG
+121	123	CD	structure_element	The error bars represent s.e.m. (c) Structural comparison of the JNK-interacting residues on MKP5-CD (PDB 1ZZW) and MKP7-CD.	FIG
+30	34	MKP5	protein	The corresponding residues on MKP5 are depicted as orange sticks, and MKP5 residues numbers are in parentheses.	FIG
+70	74	MKP5	protein	The corresponding residues on MKP5 are depicted as orange sticks, and MKP5 residues numbers are in parentheses.	FIG
+4	27	Gel filtration analysis	experimental_method	(d) Gel filtration analysis for interaction of JNK1 with MKP5-CD and MKP5-KBD. (e) GST-mediated pull-down assays for interaction of JNK1 with MKP5-CD and MKP5-KBD.	FIG
+47	51	JNK1	protein	(d) Gel filtration analysis for interaction of JNK1 with MKP5-CD and MKP5-KBD. (e) GST-mediated pull-down assays for interaction of JNK1 with MKP5-CD and MKP5-KBD.	FIG
+57	61	MKP5	protein	(d) Gel filtration analysis for interaction of JNK1 with MKP5-CD and MKP5-KBD. (e) GST-mediated pull-down assays for interaction of JNK1 with MKP5-CD and MKP5-KBD.	FIG
+62	64	CD	structure_element	(d) Gel filtration analysis for interaction of JNK1 with MKP5-CD and MKP5-KBD. (e) GST-mediated pull-down assays for interaction of JNK1 with MKP5-CD and MKP5-KBD.	FIG
+69	73	MKP5	protein	(d) Gel filtration analysis for interaction of JNK1 with MKP5-CD and MKP5-KBD. (e) GST-mediated pull-down assays for interaction of JNK1 with MKP5-CD and MKP5-KBD.	FIG
+74	77	KBD	structure_element	(d) Gel filtration analysis for interaction of JNK1 with MKP5-CD and MKP5-KBD. (e) GST-mediated pull-down assays for interaction of JNK1 with MKP5-CD and MKP5-KBD.	FIG
+83	112	GST-mediated pull-down assays	experimental_method	(d) Gel filtration analysis for interaction of JNK1 with MKP5-CD and MKP5-KBD. (e) GST-mediated pull-down assays for interaction of JNK1 with MKP5-CD and MKP5-KBD.	FIG
+132	136	JNK1	protein	(d) Gel filtration analysis for interaction of JNK1 with MKP5-CD and MKP5-KBD. (e) GST-mediated pull-down assays for interaction of JNK1 with MKP5-CD and MKP5-KBD.	FIG
+142	146	MKP5	protein	(d) Gel filtration analysis for interaction of JNK1 with MKP5-CD and MKP5-KBD. (e) GST-mediated pull-down assays for interaction of JNK1 with MKP5-CD and MKP5-KBD.	FIG
+147	149	CD	structure_element	(d) Gel filtration analysis for interaction of JNK1 with MKP5-CD and MKP5-KBD. (e) GST-mediated pull-down assays for interaction of JNK1 with MKP5-CD and MKP5-KBD.	FIG
+154	158	MKP5	protein	(d) Gel filtration analysis for interaction of JNK1 with MKP5-CD and MKP5-KBD. (e) GST-mediated pull-down assays for interaction of JNK1 with MKP5-CD and MKP5-KBD.	FIG
+159	162	KBD	structure_element	(d) Gel filtration analysis for interaction of JNK1 with MKP5-CD and MKP5-KBD. (e) GST-mediated pull-down assays for interaction of JNK1 with MKP5-CD and MKP5-KBD.	FIG
+63	72	mutations	experimental_method	The panels are arranged the same as in Fig. 2d. (f) Effects of mutations in MKP5-CD on the JNK1 dephosphorylation (mean±s.e.m., n=3).	FIG
+76	80	MKP5	protein	The panels are arranged the same as in Fig. 2d. (f) Effects of mutations in MKP5-CD on the JNK1 dephosphorylation (mean±s.e.m., n=3).	FIG
+81	83	CD	structure_element	The panels are arranged the same as in Fig. 2d. (f) Effects of mutations in MKP5-CD on the JNK1 dephosphorylation (mean±s.e.m., n=3).	FIG
+91	95	JNK1	protein	The panels are arranged the same as in Fig. 2d. (f) Effects of mutations in MKP5-CD on the JNK1 dephosphorylation (mean±s.e.m., n=3).	FIG
+15	24	mutations	experimental_method	(g) Effects of mutations in MKP5-CD on the pNPP hydrolysis reaction (mean±s.e.m., n=3).	FIG
+28	32	MKP5	protein	(g) Effects of mutations in MKP5-CD on the pNPP hydrolysis reaction (mean±s.e.m., n=3).	FIG
+33	35	CD	structure_element	(g) Effects of mutations in MKP5-CD on the pNPP hydrolysis reaction (mean±s.e.m., n=3).	FIG
+43	47	pNPP	chemical	(g) Effects of mutations in MKP5-CD on the pNPP hydrolysis reaction (mean±s.e.m., n=3).	FIG
+4	20	Pull-down assays	experimental_method	(h) Pull-down assays of MKP5-CD by GST-tagged JNK1 mutants.	FIG
+24	28	MKP5	protein	(h) Pull-down assays of MKP5-CD by GST-tagged JNK1 mutants.	FIG
+29	31	CD	structure_element	(h) Pull-down assays of MKP5-CD by GST-tagged JNK1 mutants.	FIG
+35	45	GST-tagged	protein_state	(h) Pull-down assays of MKP5-CD by GST-tagged JNK1 mutants.	FIG
+46	50	JNK1	protein	(h) Pull-down assays of MKP5-CD by GST-tagged JNK1 mutants.	FIG
+51	58	mutants	protein_state	(h) Pull-down assays of MKP5-CD by GST-tagged JNK1 mutants.	FIG