Protein function and allostery: a dynamic relationship
Protein function and allostery: a dynamic relationship
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DOI：
10.1111/j.1749-6632.2011.06319.x
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发表时间：
2012-01-01
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影响因子：
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通讯作者：
Kalodimos, Charalampos G.
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文献类型：
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作者：
Kalodimos, Charalampos G.
变构是蛋白质系统中相距较远的位点相互感知的基本过程。变构调节是一种非常有效的机制，可用于控制大多数生物过程中的蛋白质活性，包括信号转导、代谢、催化和基因调节。近年来，我们对变构基本原理的看法和理解不断丰富，而且常常被彻底重塑。对于核磁共振波谱等强大技术尤其如此，它提供了蛋白质内在运动的原子视图。在这里，我讨论了关于分解代谢激活蛋白（CAP）的最新结果，这些结果极大地改变了我们关于如何调节变构相互作用的观点。 CAP 提供了第一个经过实验鉴定的系统，表明（i）在蛋白质平均结构没有变化的情况下，变构可以通过蛋白质运动的变化来介导，以及（ii）蛋白质运动的有利变化可能会激活结构上不活跃的变构蛋白。
Allostery is a fundamental process by which distant sites within a protein system sense each other. Allosteric regulation is such an efficient mechanism that it is used to control protein activity in most biological processes, including signal transduction, metabolism, catalysis, and gene regulation. Over recent years, our view and understanding of the fundamental principles underlying allostery have been enriched and often utterly reshaped. This has been especially so for powerful techniques such as nuclear magnetic resonance spectroscopy, which offers an atomic view of the intrinsic motions of proteins. Here, I discuss recent results on the catabolite activator protein (CAP) that have drastically revised our view about how allosteric interactions are modulated. CAP has provided the first experimentally identified system showing that (i) allostery can be mediated through changes in protein motions, in the absence of changes in the mean structure of the protein, and (ii) favorable changes in protein motions may activate allosteric proteins that are otherwise structurally inactive.