2btt

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2btt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2btt OCA], [http://www.ebi.ac.uk/pdbsum/2btt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2btt RCSB]</span>
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'''NMR STRUCTURE OF MYO3-SH3 DOMAIN FROM MYOSIN-TYPE I FROM S. CEREVISIAE'''
'''NMR STRUCTURE OF MYO3-SH3 DOMAIN FROM MYOSIN-TYPE I FROM S. CEREVISIAE'''
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Revision as of 17:47, 3 May 2008

Template:STRUCTURE 2btt

NMR STRUCTURE OF MYO3-SH3 DOMAIN FROM MYOSIN-TYPE I FROM S. CEREVISIAE


Overview

SH3 domains are small protein modules that are involved in protein-protein interactions in several essential metabolic pathways. The availability of the complete genome and the limited number of clearly identifiable SH3 domains make the yeast Saccharomyces cerevisae an ideal proteomic-based model system to investigate the structural rules dictating the SH3-mediated protein interactions and to develop new tools to assist these studies. In the present work, we have determined the solution structure of the SH3 domain from Myo3 and modeled by homology that of the highly homologous Myo5, two myosins implicated in actin polymerization. We have then implemented an integrated approach that makes use of experimental and computational methods to characterize their binding properties. While accommodating their targets in the classical groove, the two domains have selectivity in both orientation and sequence specificity of the target peptides. From our study, we propose a consensus sequence that may provide a useful guideline to identify new natural partners and suggest a strategy of more general applicability that may be of use in other structural proteomic studies.

About this Structure

2BTT is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S. cerevisiae., Musi V, Birdsall B, Fernandez-Ballester G, Guerrini R, Salvatori S, Serrano L, Pastore A, Protein Sci. 2006 Apr;15(4):795-807. PMID:16600966 Page seeded by OCA on Sat May 3 20:47:14 2008

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