@article {3187,
	title = {Homology modeling of human alpha 1 beta 2 gamma 2 and house fly beta 3 GABA receptor channels and Surflex-docking of fipronil.},
	journal = {Journal of molecular modeling},
	volume = {15},
	year = {2009},
	month = {09/2009},
	pages = {1145{\textendash}1153},
	abstract = {To further explore the mechanism of selective binding of the representative gamma-aminobutyric acid receptors (GABARs) noncompetitive antagonist (NCA) fipronil to insect over mammalian GABARs, three-dimensional models of human alpha 1 beta 2 gamma 2 and house fly beta 3 GABAR were generated by homology modeling, using the cryo-electron microscopy structure of the nicotinic acetylcholine receptor (nAChR) of Torpedo marmorata as a template. Fipronil was docked into the putative binding site of the human alpha 1 beta 2 gamma 2 and house fly beta 3 receptors by Surflex-docking, and the calculated docking energies are in agreement with experimental results. The GABA receptor antagonist fipronil exhibited higher potency with house fly beta 3 GABAR than with human alpha 1 beta 2 gamma 2 GABAR. Furthermore, analyses of Surflex-docking suggest that the H-bond interaction of fipronil with Ala2 and Thr6 in the second transmembrane segment (TM2) of these GABARs plays a relatively important role in ligand selective binding. The different subunit assemblies of human alpha 1 beta 2 gamma 2 and house fly beta 3 GABARs may result in differential selectivity for fipronil.},
	keywords = {fipronil, homology modeling, house fly beta 3 GABA receptor, human alpha 1 beta 2 gamma 2 GABAA receptor, selectivity, surflex-docking},
	issn = {0948-5023},
	doi = {10.1007/s00894-009-0477-2},
	url = {http://www.ncbi.nlm.nih.gov/pubmed/19238461},
	author = {Cheng, Jin and Ju, Xiu-Lian and Xiang Yang Chen and Liu, Gen-Yan}
}
