Structures of Human Monoamine Oxidase B Complexes with Selective Noncovalent Inhibitors: Safinamide and Coumarin Analogs
Journal of Medicinal Chemistry2007Vol. 50(23), pp. 5848–5852
Citations Over TimeTop 10% of 2007 papers
Claudia Binda, Jin Wang, Leonardo Pisani, Carla Caccia, Angelo Carotti, Patricia Salvati, Dale E. Edmondson, Andrea Mattevi
Abstract
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 μM 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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