Nature2014-06-18 6:52 PM

对变构作用认识的变化 The ensemble nature of allostery

论文摘要 
 
用来了解变构作用(生物大分子将在一个结合点的效应传输给另一个结合点、随后活性发生变化的受控过程)的经典模型,一直关注的是在不同功能形式之间所观察到的独特结构和结构变化。在过去20年,人们认识到,变构作用也与动态的变化相关。在这篇文章中,Vincent Hilser及同事对动态的、内在紊乱的蛋白何以能促进变构作用进行了讨论,同时提出了将对来自不同系统的变构机制的描述加以统一的一个框架。

Abstract 

Allostery is the process by which biological macromolecules (mostly proteins) transmit the effect of binding at one site to another, often distal, functional site, allowing for regulation of activity. Recent experimental observations demonstrating that allostery can be facilitated by dynamic and intrinsically disordered proteins have resulted in a new paradigm for understanding allosteric mechanisms, which focuses on the conformational ensemble and the statistical nature of the interactions responsible for the transmission of information. Analysis of allosteric ensembles reveals a rich spectrum of regulatory strategies, as well as a framework to unify the description of allosteric mechanisms from different systems.

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