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2v5z

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==Overview==
==Overview==
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Structures 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 muM 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.
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Structures 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.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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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 Oct 4;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17915852 17915852]
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17915852 17915852]
[[Category: Amine oxidase (flavin-containing)]]
[[Category: Amine oxidase (flavin-containing)]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Caccia, C.]]
[[Category: Caccia, C.]]
[[Category: Carotti, A.]]
[[Category: Carotti, A.]]
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[[Category: Edmondson, D.E.]]
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[[Category: Edmondson, D E.]]
[[Category: Mattevi, A.]]
[[Category: Mattevi, A.]]
[[Category: Pisani, L.]]
[[Category: Pisani, L.]]
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[[Category: transmembrane]]
[[Category: transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:49:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:53:22 2008''

Revision as of 16:53, 21 February 2008


2v5z, resolution 1.60Å

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STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR SAFINAMIDE

Overview

Structures 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.

About this Structure

2V5Z is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Amine oxidase (flavin-containing), with EC number 1.4.3.4 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.

Reference

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

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