SiMMap: A web server for inferring site-moiety map to recognize interaction preferences between protein pockets and compound moieties

Yen Fu Chen, Kai Cheng Hsu, Shen Rong Lin, Wen Ching Wang, Yu Chi Huang, Jinn-Moon Yang*

*此作品的通信作者

研究成果: Article同行評審

38 引文 斯高帕斯(Scopus)

摘要

The protein-ligand interacting mechanism is essential to biological processes and drug discovery. The SiMMap server statistically derives site-moiety map with several anchors, which describe the relationship between the moiety preferences and physicochemical properties of the binding site, from the interaction profiles between query target protein and its docked (or co-crystallized) compounds. Each anchor includes three basic elements: a binding pocket with conserved interacting residues, the moiety composition of query compounds and pocket-moiety interaction type (electrostatic, hydrogen bonding or van der Waals). We provide initial validation of the site-moiety map on three targets, thymidine kinase, and estrogen receptors of antagonists and agonists. Experimental results show that an anchor is often a hot spot and the site-moiety map can help to assemble potential leads by optimal steric, hydrogen bonding and electronic moieties. When a compound highly agrees with anchors of site-moiety map, this compound often activates or inhibits the target protein. We believe that the site-moiety map is useful for drug discovery and understanding biological mechanisms. The SiMMap web server is available at http://simfam.life.nctu.edu.tw/.

原文English
文章編號gkq480
頁(從 - 到)W424–W430
頁數7
期刊Nucleic acids research
38
發行號SUPPL. 2
DOIs
出版狀態Published - 2 6月 2010

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