2btt
From Proteopedia
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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
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