title: [Mapping of active site of alcohol dehydrogenase with low-molecular ligands].
abstract: In search of an active alcohol dehydrogenase inhibitor, the structure of which may serve as the basis for a potential drug design, the active site of alcohol dehydrogenase containing NAD and Zn2+ ions was mapped using the method of molecular mechanics. Molecular docking was performed using a number of ligands containing characteristic functional groups: formate ion, ammonia, ammonium ion, methanol, and methylamine. Sites of preferable binding were revealed for each ligand and arranged in order of decreasing energy of binding to the enzyme. A comparison of the predicted ligand-binding sites and the experimental data on the location of water and inhibitor binding sites in the known structures of corresponding alcohol dehydrogenase complexes indicated a coincidence of the complex formation sites, which confirms the validity of the method and provides the requirements for a highly effective inhibitor (the pharmacophore model).
authors.affiliation: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia. ku@imb.imb.ac.ru
authors.forename: A S
authors.initials: AS
authors.lastname: Kutsenko
authors.forename: D A
authors.initials: DA
authors.lastname: Kuznetsov
authors.forename: V V
authors.initials: VV
authors.lastname: Poroĭkov
authors.forename: V G
authors.initials: VG
authors.lastname: Tumanian
mesh_terms: D000426:Alcohol Dehydrogenase / Q000037:antagonists & inhibitors / Q000737:chemistry*; D001665:Binding Sites; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000737:chemistry; D006801:Humans; D008024:Ligands; D008958:Models, Molecular
chemical_list: D004791:Enzyme Inhibitors; D008024:Ligands; D000426:Alcohol Dehydrogenase