Protein-protein docking by simulating the process of association based on predicted interface
BackgroundProtein-protein interactions are fundamental as many proteins mediate their biological function through these interactions. Many important applications follow directly from the identification of protein interface residues,such as drug design, protein mimetics engineering, elucidation of molecular pathways,and understanding of disease mechanisms. The identification of interface residues can also guide the docking process to build the structural model of protein-protein complexes.Data and MethodsInterlace predictionThere have been many efforts to predict protein-protein interaction binding sites based on the analysis of the protein surface properties. These efforts result in several webservers such as PPI Pred, PPISP, PINUP, Promate, and SPPIDER etc, to which one can submit a protein structure and is returned a predicted protein-protein interaction interface. We have developed a meta approach to improve the interface prediction based on the prediction results from these five servers 1.
Bingding Huang Michael schroeder Rebecca Wade
EML Research gGmbH, Schloss-Wolfsbrunnenweg 33, 69118 Heidelberg, Germany Bioinformatics Group, Biot Bioinformatics Group, Biotechnological Center, Technical University Dresden, Tatzberg 47-51, 01307 D EML Research gGmbH, Schloss-Wolfsbrunnenweg 33, 69118 Heidelberg, Germany
国际会议
The 7th Asia-Pacific Bioinformatics Conference(第七届亚太生物信息学大会)
北京
英文
884
2009-01-01（万方平台首次上网日期，不代表论文的发表时间）