Diversity of protein-protein interactions

被引：676

作者：

Nooren, IMA ^{[1
]}

Thornton, JM ^{[1
]}

机构：

[1] European Bioinformat Inst, EMBL, Cambridge CB10 1SD, England

来源：

EMBO JOURNAL | 2003年 / 22卷 / 14期

关键词：

complexes; protein-protein interactions; protein structures; transient interactions;

D O I：

10.1093/emboj/cdg359

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：

In this review, we discuss the structural and functional diversity of protein-protein interactions (PPIs) based primarily on protein families for which three-dimensional structural data are available. PPIs play diverse roles in biology and differ based on the composition, affinity and whether the association is permanent or transient. In vivo, the protomer's localization, concentration and local environment can affect the interaction between protomers and are vital to control the composition and oligomeric state of protein complexes. Since a change in quaternary state is often coupled with biological function or activity, transient PPIs are important biological regulators. Structural characteristics of different types of PPIs are discussed and related to their physiological function, specificity and evolution.

引用

页码：3486 / 3492

页数：7

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