Protein–protein docking with interface residue restraints  

作　　者：Hao Li Sheng-You Huang 李豪;黄胜友(School of Physics,Huazhong University of Science and Technology,Wuhan 430074,China)

机构地区：[1]School of Physics,Huazhong University of Science and Technology,Wuhan 430074,China

出　　处：《Chinese Physics B》2021年第1期19-26,共8页中国物理B（英文版）

基　　金：Project supported by the National Natural Science Foundation of China(Grant No.31670724);the Startup Grant of Huazhong University of Science and Technology。

摘　　要：The prediction of protein–protein complex structures is crucial for fundamental understanding of celluar processes and drug design. Despite significant progresses in the field, the accuracy of ab initio docking without using any experimental restraints remains relatively low. With the rapid advancement of structural biology, more and more information about binding can be derived from experimental data such as NMR experiments or chemical cross-linking. In addition, information about the residue contacts between proteins may also be derived from their sequences by using evolutionary analysis or deep learning. Here, we propose an efficient approach to incorporate interface residue restraints into protein–protein docking, which is named as HDOCKsite. Extensive evaluations on the protein–protein docking benchmark 4.0 showed that HDOCKsite significantly improved the docking performance and obtained a much higher success rate in binding mode predictions than original ab initio docking.

关 键 词：protein-protein interaction scoring function residue restraint molecular docking 

分 类 号：Q51[生物学—生物化学]