Nooren Irene M A, Thornton Janet M
European Bioinformatics Institute (EMBL-EBI), Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, UK.
EMBO J. 2003 Jul 15;22(14):3486-92. doi: 10.1093/emboj/cdg359.
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.
在本综述中,我们主要基于可获得三维结构数据的蛋白质家族,讨论蛋白质-蛋白质相互作用(PPI)的结构和功能多样性。PPI在生物学中发挥着多种作用,并且根据其组成、亲和力以及结合是永久性还是临时性而有所不同。在体内,亚基的定位、浓度和局部环境会影响亚基之间的相互作用,对于控制蛋白质复合物的组成和寡聚状态至关重要。由于四级结构的变化通常与生物学功能或活性相关联,临时性PPI是重要的生物调节因子。我们将讨论不同类型PPI的结构特征,并将其与它们的生理功能、特异性和进化联系起来。