Side-chain rotamer transitions at protein-protein interfaces
Side-chain rotamer transitions at protein-protein interfaces
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DOI：
10.1002/prot.22821
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发表时间：
2010-11-15
影响因子：
2.9
通讯作者：
Robert, Charles H.
中科院分区：
文献类型：
--
作者：
Guharoy, Mainak;Janin, Joel;Robert, Charles H.
我们比较了侧链构象的变化，伴随着蛋白质蛋白质复合物的形成，在残基形成的接口或剩余的溶剂可访问的表面的蛋白质在对接基准3.0。我们发现，界面残留物经历了显着更多的变化比其他表面残留物，这些变化更有可能将它们从一个高能量的扭转角状态转换到一个较低的能量比相反。此外，在未结合的蛋白质和复合物中，界面残基更经常被发现是在一个高能量的扭转角状态比非界面残基。由于这些差异存在于结合步骤之前，因此它们可能与特异性相关，并有助于识别用于对接预测的结合位点。Proteins 2010; 78：3219-3225. (C)2010 Wiley-Liss，Inc.
We compare the changes in side chain conformations that accompany the formation of protein protein complexes, in residues forming either the interface or the remainder of the solvent-accessible surface of the proteins in the Docking Benchmark 3.0. We find that the interface residues undergo significantly more changes than other surface residues, and these changes are more likely to convert them from a high-energy torsion angle state to a lower-energy one than the reverse. Moreover, in both the unbound proteins and the complexes, the interface residues are more frequently found to be in a high-energy torsion angle state than the noninterface residues. As these differences exist before the binding step, they may be relevant to specificity and help in identifying binding sites for docking predictions. Proteins 2010; 78:3219-3225. (C) 2010 Wiley-Liss, Inc.