Identification of hot spot residues at protein-protein interface

被引:30
|
作者
Li, Lei [1 ]
Zhao, Bing [1 ]
Cui, Zhanhua [1 ]
Gan, Jacob [1 ]
Sakharkar, Meena Kishore [1 ]
Kangueane, Pandjassarame [1 ]
机构
[1] Nanyang Technol Univ, Sch Mech & Aerosp Engn, Singapore 639798, Singapore
关键词
protein-protein interaction; interface analysis; hot spot residues; inter-atomic interaction;
D O I
10.6026/97320630001121
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:121 / +
页数:13
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