Uncovering new aspects of protein interactions through analysis of specificity landscapes in peptide recognition domains

被引:11
作者
Gfeller, David [1 ]
机构
[1] SIB, CH-1015 Lausanne, Switzerland
来源
FEBS LETTERS | 2012年 / 586卷 / 17期
关键词
Binding specificity; Peptide recognition domain; Protein interaction; STRUCTURE-BASED PREDICTION; PROLINE-RICH LIGANDS; SRC HOMOLOGY 3; PDZ DOMAIN; SH3; DOMAINS; INTERACTION NETWORKS; BINDING DOMAIN; TRANSLATIONAL INITIATION; SACCHAROMYCES-CEREVISIAE; SH3-LIGAND INTERACTIONS;
D O I
10.1016/j.febslet.2012.03.054
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
Protein interactions underlie all biological processes. An important class of protein interactions, often observed in signaling pathways, consists of peptide recognition domains binding short protein segments on the surface of their target proteins. Recent developments in experimental techniques have uncovered many such interactions and shed new lights on their specificity. To analyze these data, novel computational methods have been introduced that can accurately describe the specificity landscape of peptide recognition domains and predict new interactions. Combining large-scale analysis of binding specificity data with structure-based modeling can further reveal new biological insights into the molecular recognition events underlying signaling pathways. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:2764 / 2772
页数:9
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