The architecture of the binding site in redox protein complexes: Implications for fast dissociation
The architecture of the binding site in redox protein complexes: Implications for fast dissociation
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DOI：
10.1002/prot.20043
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发表时间：
2004-05-15
影响因子：
2.9
通讯作者：
Carrondo, MA
中科院分区：
文献类型：
--
作者：
Crowley, PB;Carrondo, MA
蛋白质间电子传递的特点是蛋白质相互作用的毫秒级时间尺度。这种短暂的相遇是由极高的复合物解离速率所保证的。氧化还原蛋白复合物的可用晶体结构的计算分析揭示了有利于快速解离的结合位点的特征。特别是，复杂的接口示出具有低的几何互补性和不良的包装。这些特征与快速解离的必要性是一致的，因为没有紧密堆积有利于界面的溶剂化和复合物的破坏。(C)2004 Wiley-Liss，Inc.
Interprotein electron transfer is characterized by protein interactions on the millisecond time scale. Such transient encounters are ensured by extremely high rates of complex dissociation. Computational analysis of the available crystal structures of redox protein complexes reveals features of the binding site that favor fast dissociation. In particular, the complex interface is shown to have low geometric complementarity and poor packing. These features are consistent with the necessity for fast dissociation since the absence of close packing facilitates solvation of the interface and disruption of the complex. (C) 2004 Wiley-Liss, Inc.