1ojc

From Proteopedia

Revision as of 13:51, 30 October 2007

HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH N-(2-AMINOETHYL)-P-CHLOROBENZAMIDE

Overview

Monoamine oxidase B (MAO-B) is an outer mitochondrial membrane-bound, enzyme that catalyzes the oxidative deamination of arylalkylamine, neurotransmitters and has been a target for a number of clinically used, drug inhibitors. The 1.7-A structure of the reversible isatin-MAO-B, complex has been determined; it forms a basis for the interpretation of, the enzyme's structure when bound to either reversible or irreversible, inhibitors. 1,4-Diphenyl-2-butene is found to be a reversible MAO-B, inhibitor, which occupies both the entrance and substrate cavity space in, the enzyme. Comparison of these two structures identifies Ile-199 as a, "gate" between the two cavities. Rotation of the side chain allows for, either separation or fusion of the two cavities. Inhibition of the enzyme, with ... [(full description)]

About this Structure

1OJC is a [Single protein] structure of sequence from [Homo sapiens] with FAD as [ligand]. Active as [Amine oxidase (flavin-containing)], with EC number [1.4.3.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures., Binda C, Li M, Hubalek F, Restelli N, Edmondson DE, Mattevi A, Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):9750-5. Epub 2003 Aug 11. PMID:12913124

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