Global low-frequency motions in protein allostery: CAP as a model system.
Global low-frequency motions in protein allostery: CAP as a model system.
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DOI：
10.1007/s12551-015-0163-9
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发表时间：
2015
影响因子：
--
通讯作者：
Cann, Martin J
中科院分区：
文献类型：
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作者：
Townsend, Philip D;Rodgers, Thomas L;Pohl, Ehmke;Wilson, Mark R;McLeish, Tom C B;Cann, Martin J
变构是配体与蛋白质结合改变其在远处位点的活性的基本过程。有大量证据表明变构协同性可以通过调节蛋白质动力学而无需构象变化来传达。大肠杆菌的分解代谢激活蛋白（CAP）是熵驱动变构的重要实验范例。在这里，我们讨论最近的实验支持的理论分析，强调全局低频动态在 CAP 变构中的作用，并确定变构如何作为配体结合的全局低频蛋白质波动变化的自然结果而出现。
Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformational change. The Catabolite Activator Protein (CAP) of Escherichia coli is an important experimental exemplar for entropically driven allostery. Here we discuss recent experimentally supported theoretical analysis that highlights the role of global low-frequency dynamics in allostery in CAP and identify how allostery arises as a natural consequence of changes in global low-frequency protein fluctuations on ligand binding.