Computer modelling of monoaminoxidases

Veselovsky A.V.1, Ivanov A.S.1, Medvedev A.E.1

1. Institute of Biomedical Chemistry, Moscow, Russia
Section: Review
DOI: 10.18097/PBMC20156102265      PubMed Id: 25978392
Year: 2015  Volume: 61  Issue: 2  Pages: 265-271
The article summarized results of studies on active site structures of monoamine oxidases (MAO) performed in the Institute of Biomedical Chemistry (Russia) by computer modelling approaches. MAO, catalyzing the reaction of oxidative deamination of major neurotransmitter monoamines, exists in two highly homologous forms, MAO A and MAO B, distinguished by substrate specificity and inhibitor selectivity. The development of approaches for active site modelling of these enzymes (with unknown three-dimensional structures) started from analysis of relationship between the geometrical sizes of rigid indole and isatin derivatives and their inhibitory activity. These studies resulted in molding of the active site structures of MAO A and MAO B. These molds reflect the sizes and shapes of active sites of these enzymes. These mold models have been used for virtual screening of molecular databases for new inhibitors. The models obtained at different stages ofMAO investigations have been compared with recently appeared three-dimensional structures of MAO A and MAO B.
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Keywords: monoamine oxidase, MAO, computer modelling, active site, inhibitors

Veselovsky, A. V., Ivanov, A. S., Medvedev, A. E. (2015). Computer modelling of monoaminoxidases. Biomeditsinskaya Khimiya, 61(2), 265-271.
This paper is also available as the English translation: 10.1134/S1990750815030105
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