page_title: CSNK1D
section_title: Structure
hierarchical_section_title: CSNK1D / Structure
caption_attribution_description: English: Three-dimensional structure of human CK1δ. While the structure of the N-lobe mainly consists of β-sheet strands, the larger C-terminal lobe is mainly composed by α-helices and loop structures. The DFG motif is located within loop L-89. A recognition motif for the binding of phosphorylated substrates has been identified by detection of a tungstate-binding domain, indicated by W1. The position of the catalytic loop (L-67) is marked with the asterisk (PMID: 8648628, 7889932). The figure was created by using CK1δ crystallization data created by Ben-neriah et al. (PMID: 30146162), deposited in the protein data bank (PDB) with ID 6GZM.
context_page_description: Casein kinase I isoform delta also known as CKI-delta or CK1δ is an enzyme that in humans is encoded by the gene CSNK1D, which is located on chromosome 17. It is a member of the CK1 family of serine/threonine specific eukaryotic protein kinases encompassing seven distinct isoforms as well as various post-transcriptionally processed splice variants in mammalians. Meanwhile, CK1δ homologous proteins have been isolated from organisms like yeast, basidiomycetes, plants, algae, and protozoa.
context_section_description: Like eukaryotic protein kinases (ePKs) the different isoforms of the CK1 family consist of a N-terminal and a C-terminal lobe (N- and C-lobe, respectively), which are connected via a hinge region. While the N-lobe is mainly composed by β-sheet strands, the larger C-lobe predominantly consists of α-helical and loop structures. Between both lobes a catalytic cleft is formed, accommodating substrates and ATP for the kinase reaction.
caption: Figure 1: Three-dimensional structure of human CK1δ. While the structure of the N-lobe mainly consists of β-sheet strands, the larger C-terminal lobe is mainly composed by α-helices and loop structures. The DFG motif is located within loop L-89. A recognition motif for the binding of phosphorylated substrates has been identified by detection of a tungstate-binding domain, indicated by W1. The position of the catalytic loop (L-67) is marked with the asterisk.[26][27] The figure was created by using CK1δ crystallization data created by Ben-neriah et al.,[28] deposited in the protein data bank (PDB) with ID 6GZM.
exif: {}