Function and structure of inherently disordered proteins

被引：755

作者：

Dunker, A. Keith ^{[4
]}

Silman, Israel ^{[2
,5
]}

Uversky, Vladimir N. ^{[3
,4
,6
]}

Sussman, Joel L. ^{[1
,2
]}

机构：

[1] Weizmann Inst Sci, Dept Biol Struct, IL-76100 Rehovot, Israel

[2] Weizmann Inst Sci, Israel Struct Prote Ctr, IL-76100 Rehovot, Israel

[3] Indiana Univ, Inst Intrinsically Disordered Prot Res, Ctr Computat Biol & Bioinformat, Dept Biochem & Mol Biol,Sch Med, Indianapolis, IN 46202 USA

[4] Indiana Univ, Sch Informat, Ctr Computat Biol & Bioinformat, Inst Intrinsically Disordered Prot Res, Indianapolis, IN 46202 USA

[5] Weizmann Inst Sci, Dept Neurobiol, IL-76100 Rehovot, Israel

[6] Russian Acad Sci, Inst Biol Instrumentat, Moscow 142290, Russia

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2008年 / 18卷 / 06期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/j.sbi.2008.10.002

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：

The application of bioinformatics methodologies to proteins inherently lacking 3D structure has brought increased attention to these macromolecules. Here topics concerning these proteins are discussed, including their prediction from amino acid sequence, their enrichment in eukaryotes compared to prokaryotes, their more rapid evolution compared to structured proteins, their organization into specific groups, their structural preferences, their half-lives in cells, their contributions to signaling diversity (via high contents of multiple-partner binding sites, post-translational modifications, and alternative splicing), their distinct functional repertoire compared to that of structured proteins, and their involvement in diseases.

引用

页码：756 / 764

页数：9

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