Structure and function of WD40 domain proteins

被引：474

作者：

Xu, Chao ^{[1
]}

Min, Jinrong ^{[1
,2
]}

机构：

[1] Univ Toronto, Struct Genom Consortium, Toronto, ON M5G 1L7, Canada

[2] Univ Toronto, Dept Physiol, Toronto, ON M5S 1A8, Canada

来源：

PROTEIN & CELL | 2011年 / 2卷 / 03期

基金：

英国惠康基金;

关键词：

WD40; beta-propeller; protein-protein interaction; scaffold; post-translational modification; UBIQUITIN LIGASE MACHINERY; HISTONE H3; MOLECULAR RECOGNITION; SPINDLE CHECKPOINT; CRYSTAL-STRUCTURE; BINDING-PROTEINS; REPEAT PROTEIN; DNA-DAMAGE; METHYLTRANSFERASE ACTIVITY; WD40-REPEAT PROTEINS;

D O I：

10.1007/s13238-011-1018-1

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The WD40 domain exhibits a beta-propeller architecture, often comprising seven blades. The WD40 domain is one of the most abundant domains and also among the top interacting domains in eukaryotic genomes. In this review, we will discuss the identification, definition and architecture of the WD40 domains. WD40 domain proteins are involved in a large variety of cellular processes, in which WD40 domains function as a protein-protein or protein-DNA interaction platform. WD40 domain mediates molecular recognition events mainly through the smaller top surface, but also through the bottom surface and sides. So far, no WD40 domain has been found to display enzymatic activity. We will also discuss the different binding modes exhibited by the large versatile family of WD40 domain proteins. In the last part of this review, we will discuss how post-translational modifications are recognized by WD40 domain proteins.

引用

页码：202 / 214

页数：13

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