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Homology models of the ligand binding domain of the wild-type and Y151S mutant brown planthopper {Nilaparvata lugens)α1 and rat(Rattus norvegicus)β2 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 mutantα1β2 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.
Homology models of the ligand binding domain of the wild-type and Y151S mutant brown planthopper {Nilaparvata lugens) α1 and rat (Rattus norvegicus) β2 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 α1β2 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.