Identification of hot spot residues at protein-protein interface.
Identification of hot spot residues at protein-protein interface.
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DOI：
10.6026/97320630001121
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发表时间：
2006-04-04
期刊：
影响因子：
1.9
通讯作者：
Kangueane P
中科院分区：
文献类型：
--
作者：
Li L;Zhao B;Cui Z;Gan J;Sakharkar MK;Kangueane P
蛋白质-蛋白质相互作用的结合自由能主要由热点（高能）界面残基贡献。这里我们 通过使用296个丙氨酸突变界面的数据集检查原子间侧链-侧链相互作用来研究热点的特征 残基结果表明，热点参与强有力的和积极有利的侧链-侧链相互作用。随后，我们描述了一部小说， 然而简单的“热点”预测模型具有与许多可用方法类似的精度。该模型还表明，有效地区分 特异性蛋白质-蛋白质相互作用与非特异性相互作用。
It is known that binding free energy of protein-protein interaction is mainly contributed by hot spot (high energy) interface residues. Here, we investigate the characteristics of hot spots by examining inter-atomic sidechain-sidechain interactions using a dataset of 296 alanine-mutated interface residues. Results show that hot spots participate in strong and energetically favorable sidechain-sidechain interactions. Subsequently, we describe a novel, yet simple ‘hot spot’ prediction model with an accuracy that is similar to many available approaches. The model is also shown to efficiently distinguish specific protein-protein interactions from non-specific interactions.