Structural and functional analysis of Saccharomyces cerevisiae mob protein
Subtitle: dimerization and binding to the DBF2 protein kinase .
Published: 2005
Language: eng
Number of pages: 60
Description: Mob proteins are a small family of highly conserved, non-catalytic proteins that are found in all eukaryotes. Prior to this work, structures of human and Xenopus Mob1 have been determined. I have now solved the X-ray crystal structure of S. cerevisiae Mob1 (residues 79-319), which includes the N-terminal region (residues 79-133) not included in previous structural studies. Within the N-terminal region are two novel structural elements. A novel helix, denoted helix H0, is found to bind a second Mobl molecule in an intermolecular manner, forming an interdigitated Mob1 homodimer. Furthermore, a strand, denoted strand S0, is found to bind Mob1 in an intermolecular manner across the putative Dbf2 binding site of the Mob1 core domain. Biochemical and genetic analysis has revealed that the N-terminal region of Mob1 is important for interaction with Mob2 in vivo and for high affinity interaction with the Dbf2 protein kinase.
Notes: Source: Masters Abstracts International, Volume: 44-02, page: 0764.

Thesis (M.Sc.)--University of Toronto, 2005.

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