Department of Biology and T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, USA.
Nature. 2014 Apr 17;508(7496):331-9. doi: 10.1038/nature13001.
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.
变构作用是生物大分子(主要是蛋白质)将结合在一个位置的效应传递到另一个位置(通常是远处的功能位点)的过程,从而实现活性的调节。最近的实验观察表明,动态和固有无序的蛋白质可以促进变构作用,这为理解变构机制提供了一个新的范例,该范例侧重于构象集合和负责信息传递的相互作用的统计性质。变构集合的分析揭示了丰富的调控策略,以及统一不同系统的变构机制描述的框架。