科研之友
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摘要
Homology models of the ligand binding domain of the wild-type and Y151S mutant brown planthopper (Nilaparvata lugens) alpha 1 and rat (Rattus norvegicus) beta 2 nicotinic acetylcholine receptor (nAChR) subunits were generated based on the crystal structure of acetylcholine binding protein of Lymnaea stagnalis. Neonicotinoid insecticide imidacloprid was docked into the putative binding site of wild-type and mutant alpha 1 beta 2 dimeric receptors by Surflex-docking, and the calculated docking energies were in agreement with experimental results. The resistance mechanisms and corresponding binding modes of imidacloprid on nAChRs containing the Y151S target-site mutation were discussed.
- 出版日期2010-4
- 单位中国农业科学院; 武汉工程大学
