Allostery: absence of a change in shape does not imply that allostery is not at play.
Allostery: absence of a change in shape does not imply that allostery is not at play.
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DOI：
10.1016/j.jmb.2008.02.034
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发表时间：
2008-04
影响因子：
5.6
通讯作者：
Chung-Jung Tsai;A. del Sol;R. Nussinov
中科院分区：
文献类型：
--
作者：
Chung-Jung Tsai;A. del Sol;R. Nussinov
变构对于受控催化、信号传递、受体运输、基因开启和关闭以及细胞凋亡是必不可少的。它控制着生物体对环境和代谢线索的反应，决定了细胞网络中短暂的伴侣相互作用。教科书告诉我们，变构是蛋白质表面上一个位点的形状变化，这是由配体与另一个位点结合引起的。几年来，人们普遍认为形状的改变不是由诱导引起的，而只是因为更大的蛋白质群体呈现了它。目前的数据表明，虽然侧链可以重新定向和重新连接，但变构甚至可能不涉及（主链）形状的改变。假设焓的变化不会逆转自由能的变化，因为熵的变化，熵是主要负责绑定。
Allostery is essential for controlled catalysis, signal transmission, receptor trafficking, turning genes on and off, and apoptosis. It governs the organism's response to environmental and metabolic cues, dictating transient partner interactions in the cellular network. Textbooks taught us that allostery is a change of shape at one site on the protein surface brought about by ligand binding to another. For several years, it has been broadly accepted that the change of shape is not induced; rather, it is observed simply because a larger protein population presents it. Current data indicate that while side chains can reorient and rewire, allostery may not even involve a change of (backbone) shape. Assuming that the enthalpy change does not reverse the free-energy change due to the change in entropy, entropy is mainly responsible for binding.