| Autor: |
Veselovsky AV; Institute of Biomedical Chemistry, Moscow, Russia., Ivanov AS; Institute of Biomedical Chemistry, Moscow, Russia., Medvedev AE; Institute of Biomedical Chemistry, Moscow, Russia. |
| Jazyk: |
ruština |
| Zdroj: |
Biomeditsinskaia khimiia [Biomed Khim] 2015 Mar-Apr; Vol. 61 (2), pp. 265-71. |
| DOI: |
10.18097/PBMC20156102265 |
| Abstrakt: |
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 of MAO investigations have been compared with recently appeared three-dimensional structures of MAO A and MAO B. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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