Homology Modeling of Human 5-HT2a Serotonin Receptor
We have developed a homology model of the human serotonin 5-HT2a receptor, a G protein-coupled receptor, based on the high-resolution crystal structure of the human beta-2 adrenergic receptor (2RH1). The homology model was built using the Biopolymer module in SYBYL, minimized with CHARMM, and subjected to validation with PROCHECK. A set of ligands comprising agonists and antagonists (both endogenous ligands and marketed drugs) were blind docked into the receptor using AutoDock 4.2, and all ligands were found to dock into the orthosteric binding site. The ligand-receptor binding interactions on the orthosteric binding sites were then investigated. The binding modes were compared with the site-directed mutagenesis data and a good correlation with the experimental data was observed. Therefore, we concluded that this model can be used for future drug design and discovery studies.
Serotonin receptor 5-HT2A receptor homology model G protein-coupled receptor docking
BeowKeat Yap Michael J. C. Buckle Stephen W. Doughty
Department of Pharmacy University of Malaya Kuala Lumpur, Malaysia The School of Pharmacy University of Nottingham Malaysia Campus Selangor, Malaysia
国际会议
三亚
英文
340-344
2011-03-25（万方平台首次上网日期，不代表论文的发表时间）