Protein interactions in 3D: From interface evolution to drug discovery

被引:20
作者
Winter, Christof [1 ]
Henschel, Andreas [2 ]
Tuukkanen, Anne [1 ]
Schroeder, Michael [1 ]
机构
[1] Tech Univ Dresden, Ctr Biotechnol, D-01307 Dresden, Germany
[2] Masdar Inst Sci & Technol, Abu Dhabi, U Arab Emirates
关键词
Structural protein interaction; Databases; Evolution; Drug repositioning; Protein interaction prediction; STRUCTURALLY CONSERVED RESIDUES; HOT-SPOTS; CRYSTAL-STRUCTURE; BINDING-SITES; COMPREHENSIVE DATABASE; WEB SERVER; PREDICTION; INHIBITION; SEQUENCE; DOCKING;
D O I
10.1016/j.jsb.2012.04.009
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
Over the past 10 years, much research has been dedicated to the understanding of protein interactions. Large-scale experiments to elucidate the global structure of protein interaction networks have been complemented by detailed studies of protein interaction interfaces. Understanding the evolution of interfaces allows one to identify convergently evolved interfaces which are evolutionary unrelated but share a few key residues and hence have common binding partners. Understanding interaction interfaces and their evolution is an important basis for pharmaceutical applications in drug discovery. Here, we review the algorithms and databases on 3D protein interactions and discuss in detail applications in interface evolution, drug discovery, and interface prediction. (C) 2012 Elsevier Inc. All rights reserved.
引用
收藏
页码:347 / 358
页数:12
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