2v60 | pdb_00002v60
From Proteopedia
STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR 7-(3-CHLOROBENZYLOXY)-4-CARBOXALDEHYDE-COUMARIN
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStructures of human monoamine oxidase B (MAO B) in complex with safinamide and two coumarin derivatives, all sharing a common benzyloxy substituent, were determined by X-ray crystallography. These compounds competitively inhibit MAO B with Ki values in the 0.1-0.5 microM range that are 30-700-fold lower than those observed with MAO A. The inhibitors bind noncovalently to MAO B, occupying both the entrance and the substrate cavities and showing a similarly oriented benzyloxy substituent. Structures of human monoamine oxidase B complexes with selective noncovalent inhibitors: safinamide and coumarin analogs.,Binda C, Wang J, Pisani L, Caccia C, Carotti A, Salvati P, Edmondson DE, Mattevi A J Med Chem. 2007 Nov 15;50(23):5848-52. Epub 2007 Oct 4. PMID:17915852[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 15:09, 19 January 2015.