Transient Protein-Protein Interactions: Structural, Functional, and Network Properties

被引：394

作者：

Perkins, James R. ^{[1
]}

Diboun, Ilhem ^{[1
]}

Dessailly, Benoit H. ^{[1
]}

Lees, Jon G. ^{[1
]}

Orengo, Christine ^{[1
]}

机构：

[1] UCL, Dept Struct & Mol Biol, London WC1E 6BT, England

来源：

STRUCTURE | 2010年 / 18卷 / 10期

关键词：

BIMOLECULAR FLUORESCENCE COMPLEMENTATION; LINEAR MOTIFS; INTRINSIC DISORDER; DATA INTEGRATION; CROSS-LINKING; HUB PROTEINS; COMPLEX; BINDING; PREDICTION; EVOLUTION;

D O I：

10.1016/j.str.2010.08.007

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：

Transient interactions, which involve protein interactions that are formed and broken easily, are important in many aspects of cellular function. Here we describe structural and functional properties of transient interactions between globular domains and between globular domains, short peptides, and disordered regions. The importance of posttranslational modifications in transient interactions is also considered. We review techniques used in the detection of the different types of transient protein-protein interactions. We also look at the role of transient interactions within protein-protein interaction networks and consider their contribution to different aspects of these networks.

引用

页码：1233 / 1243

页数：11

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