Intrinsically disordered proteins: administration not executive

被引：10

作者：

Williamson, Mike P. ^{[1
]}

Potts, Jennifer R. ^{[2
]}

机构：

[1] Univ Sheffield, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England

[2] Univ York, Dept Biol, York YO10 5DD, N Yorkshire, England

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2012年 / 40卷

基金：

英国医学研究理事会;

关键词：

flexibility; globular protein; intrinsically disordered protein (IDP); protein evolution; secondary structure; RESIDUAL DIPOLAR COUPLINGS; UNSTRUCTURED PROTEINS; STRUCTURAL DISORDER; ALPHA-SYNUCLEIN; BINDING; DOMAINS; MOTIFS; INTERPLAY; ALLOSTERY; NETWORKS;

D O I：

10.1042/BST20120188

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：

IDPs (intrinsically disordered proteins) are common in eukaryotic genomes and have regulatory roles. In the cell, they are disordered, although not completely random. They bind weakly, but specifically, often remaining partially disordered even when bound. Whereas folded globular proteins have 'executive' roles in the cell, IDPs have an essential administrative function, making sure that the executive functions are properly co-ordinated. This makes them a good target for pharmaceutical intervention.

引用

页码：945 / 949

页数：5

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