title: Molecular modeling of the alpha9alpha10 nicotinic acetylcholine receptor subtype.
abstract: This study reports the comparative molecular modeling, docking and dynamic simulations of human alpha9alpha10 nicotinic acetylcholine receptors complexed with acetylcholine, nicotine and alpha-conotoxin RgIA, using as templates the crystal structures of Aplysia californica and Lymnaea stagnalis acetylcholine binding proteins. The molecular dynamics simulations showed that Arg112 in the complementary alpha10(-) subunit, is a determinant for recognition in the site that binds small ligands. However, Glu195 in the principal alpha9(+), and Asp114 in the complementary alpha10(-) subunit, might confer the potency and selectivity to alpha-conotoxin RgIA when interacting with Arg7 and Arg9 of this ligand.
authors.affiliation: Department of Chemistry, Faculty of Sciences, University of Chile, Casilla, Santiago, Chile.
authors.forename: Edwin G
authors.initials: EG
authors.lastname: Pérez
authors.forename: Bruce K
authors.initials: BK
authors.lastname: Cassels
authors.forename: Gerald
authors.initials: G
authors.lastname: Zapata-Torres
mesh_terms: D000109:Acetylcholine / Q000737:chemistry; D000596:Amino Acids; D000818:Animals; D001048:Aplysia / Q000737:chemistry; D001665:Binding Sites; D003198:Computer Simulation; D020916:Conotoxins / Q000737:chemistry; D006801:Humans; D008195:Lymnaea / Q000737:chemistry; D008958:Models, Molecular; D009538:Nicotine / Q000737:chemistry; D011485:Protein Binding; D011978:Receptors, Nicotinic / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D020916:Conotoxins; D011978:Receptors, Nicotinic; C443079:nAChR alpha9; D009538:Nicotine; D000109:Acetylcholine