Hydration of protein-protein interfaces
Hydration of protein-protein interfaces
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DOI：
10.1002/prot.20478
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发表时间：
2005-07-01
影响因子：
2.9
通讯作者：
Janin, J
中科院分区：
文献类型：
--
作者：
Rodier, F;Bahadur, RP;Janin, J
我们提出了一个分析的水分子固定在蛋白质-蛋白质界面的115同源二聚体蛋白质和46蛋白质-蛋白质复合物，并比较它们与173大晶体包装接口代表非特异性相互作用。平均每1000埃的界面面积有15个沃茨（2），晶体堆积界面比同二聚体和复合物的特定界面更水合，后者每1000埃有10-11个沃茨（2），反映了晶体堆积界面更亲水的组成。观察到非常不同的水合模式：水分子可以在保持“干燥”的界面周围形成环，或者它们可以渗透“湿”界面。大多数特定的界面是干的，大多数晶体堆积界面是湿的，但反例存在于这两类。水分子在界面处与蛋白质基团形成氢键，优选主链羰基和Glu、Asp和Arg的带电侧链。这些相互作用在特异性和非特异性界面中基本相同，并且与蛋白质表面上其他地方观察到的相互作用非常相似。水介导的极性相互作用是丰富的直接蛋白质-蛋白质氢键的接口，他们可能有助于组装的稳定性。(c)2005 Wiley-Liss，Inc.
We present an analysis of the water molecules immobilized at the protein-protein interfaces of 115 homodimeric proteins and 46 protein-protein complexes, and compare them with 173 large crystal packing interfaces representing nonspecific interactions. With an average of 15 waters per 1000 angstrom(2) of interface area, the crystal packing interfaces are more hydrated than the specific interfaces of homodimers and complexes, which have 10-11 waters per 1000 angstrom(2), reflecting the more hydrophilic composition of crystal packing interfaces. Very different patterns of hydration are observed: Water molecules may form a ring around interfaces that remain "dry," or they may permeate "wet" interfaces. A majority of the specific interfaces are dry and most of the crystal packing interfaces are wet, but counterexamples exist in both categories. Water molecules at interfaces form hydrogen bonds with protein groups, with a preference for the main-chain carbonyl and the charged side-chains of Glu, Asp, and Arg. These interactions are essentially the same in specific and nonspecific interfaces, and very similar to those observed elsewhere on the protein surface. Water-mediated polar interactions are as abundant at the interfaces as direct protein-protein hydrogen bonds, and they may contribute to the stability of the assembly. (c) 2005 Wiley-Liss, Inc.