Expanding the Paradigm: Intrinsically Disordered Proteins and Allosteric Regulation

被引:98
作者
Berlow, Rebecca B.
Dyson, H. Jane
Wright, Peter E. [1 ]
机构
[1] Scripps Res Inst, Dept Integrat Struct & Computat Biol, 10550 North Torrey Pines Rd, La Jolla, CA 92037 USA
基金
美国国家卫生研究院;
关键词
CREB-BINDING PROTEIN; ETS-1; DNA-BINDING; HYPOXIA-INDUCIBLE FACTOR-1-ALPHA; TRANSCRIPTION FACTOR-BINDING; STRUCTURAL BASIS; KIX DOMAIN; FACILITATED DISSOCIATION; POSTTRANSLATIONAL MODIFICATIONS; CONDITIONAL COOPERATIVITY; CONFORMATIONAL DYNAMICS;
D O I
10.1016/j.jmb.2018.04.003
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
Allosteric regulatory processes are implicated at all levels of biological function. Recent advances in our understanding of the diverse and functionally significant class of intrinsically disordered proteins have identified a multitude of ways in which disordered proteins function within the confines of the allosteric paradigm. Allostery within or mediated by intrinsically disordered proteins ensures robust and efficient signal integration through mechanisms that would be extremely unfavorable or even impossible for globular protein interaction partners. Here, we highlight recent examples that indicate the breadth of biological outcomes that can be achieved through allosteric regulation by intrinsically disordered proteins. Ongoing and future work in this rapidly evolving area of research will expand our appreciation of the central role of intrinsically disordered proteins in ensuring the fidelity and efficiency of cellular regulation. (C) 2018 Elsevier Ltd. All rights reserved.
引用
收藏
页码:2309 / 2320
页数:12
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