2BTT

NMR Structure of MYO3-SH3 domain from Myosin-typeI from S. cerevisiae

2BTT の概要

• エントリーDOI: 10.2210/pdb2btt/pdb
• 関連するPDBエントリー: 1RUW
• NMR情報: BMRB: 6197
• 分子名称: MYOSIN-3 ISOFORM (1 entity in total)
• 機能のキーワード: sh3 domain, myosin-type i, muscle protein, contractile protein, actin-binding, atp-binding, motor protein, myosin, nucleotide-binding, phosphorylation
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7588.49

構造登録者

Musi, V.,Birdsall, B.,Pastore, A. (登録日: 2005-06-06, 公開日: 2006-04-12, 最終更新日: 2024-04-24)

主引用文献

Musi, V.,Birdsall, B.,Fernandez-Ballester, G.,Guerrini, R.,Salvatori, S.,Serrano, L.,Pastore, A.
New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S. cerevisiae.
Protein Sci., 15:795-807, 2006

PubMed Abstract: 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.

PubMed: 16600966
DOI: 10.1110/ps.051785506

実験手法

SOLUTION NMR