Improving CAPRI predictions:: Optimized desolvation for rigid-body docking

被引:43
作者
Fernández-Recio, J
Abagyan, R
Totrov, M
机构
[1] Molsoft LLC, La Jolla, CA 92037 USA
[2] Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England
[3] Scripps Res Inst, Dept Mol Biol, La Jolla, CA USA
关键词
D O I
10.1002/prot.20575
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The ICM Docking and Interface Side-Chain Optimization (ICM-DISCO) showed promising predictive results during the first CAPRI experiment by successfully finding medium- or high-accuracy models in 3 of the 7 targets. A key factor was the ability to recognize near-native rigid-body geometries in a relatively low number of alternative docking poses, together with the successful refinement of the rigid-body docking interfaces. Since then, we have focused on improving the scoring function to optimally discriminate the near-native rigid-body conformations. For that, we have defined a new desolvation descriptor for rigid-body docking, based on atomic solvation parameters (ASPs) derived from octanol-water transfer experiments. This and other new approaches have been gradually incorporated into our docking procedure during our participation on the second CAPRI experiment. Overall, we produced reasonable models for 8 of the 9 official targets. Especially encouraging were those cases in which a homology model of 1 of the subunits had to be used during the docking simulations. And not less gratifying has been the successful prediction of antibody-antigen targets in a completely automatic, unrestrained fashion. In summary, our success rate (89%) shows a consistent improvement over the previous CAPRI rounds, and suggests that a correct desolvation description is key for improved protein-protein docking predictions. (c) 2005 Wiley-Liss, Inc.
引用
收藏
页码:308 / 313
页数:6
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