SH3 domain ligand binding: What's the consensus and where's the specificity?

被引：186
作者：
Saksela, Kalle [1 ,2 ]
Permi, Perttu [3 ]
机构：
[1] Univ Helsinki, Haartman Inst, Dept Virol, FI-00014 Helsinki, Finland
[2] Univ Helsinki, Cent Hosp, HUSLAB, FI-00014 Helsinki, Finland
[3] Univ Helsinki, Inst Biotechnol, Program Struct Biol & Biophys, FI-00014 Helsinki, Finland
来源：
FEBS LETTERS | 2012年 / 586卷 / 17期
关键词：
SH3; domain; Specificity zone; Binding motifs; Atypical ligand; PROLINE-RICH PEPTIDES; HIGH-AFFINITY PEPTIDE; STRUCTURAL BASIS; CRYSTAL-STRUCTURE; SH3-LIGAND INTERACTIONS; BETA-PIX; RECOGNITION; MOTIF; MODE; IDENTIFICATION;
D O I：
10.1016/j.febslet.2012.04.042
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
An increasing number of SH3 domain-ligand interactions continue to be described that involve the conserved peptide-binding surface of SH3, but structurally deviate substantially from canonical docking of consensus motif-containing SH3 ligands. Indeed, it appears that that the relative frequency and importance of these types of interactions may have been underestimated. Instead of atypical, we propose referring to such peptides as type I or II (depending on the binding orientation) non-consensus ligands. Here we discuss the structural basis of non-consensus SH3 ligand binding and the dominant role of the SH3 domain specificity zone in selective target recognition, and review some of the best-characterized examples of such interactions. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码：2609 / 2614
页数：6
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