Molecular Dynamics Study of Triazole Derivative Binding to the Active Site of Imidazole Glycerol Phosphate Dehydratase from Mycobacterium tuberculosis
- Авторы: Agapova Y.K.1, Timofeev V.I.1,2, Komolov A.S.1
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Учреждения:
- National Research Center “Kurchatov Institute”
- Shubnikov Institute of Crystallography of the Federal Scientific Research Centre “Crystallography and Photonics,” Russian Academy of Sciences
- Выпуск: Том 64, № 4 (2019)
- Страницы: 608-610
- Раздел: Structure of Macromolecular Compounds
- URL: https://journals.rcsi.science/1063-7745/article/view/194099
- DOI: https://doi.org/10.1134/S1063774519040023
- ID: 194099
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Аннотация
Models of imidazole glycerol phosphate dehydratase from Mycobacterium tuberculosis in complexes with a number of triazole derivatives, which are known to act as inhibitors of the homologous enzyme of plant origin, were constructed. Molecular dynamics studies showed that these compounds are stably bound to the active site of imidazole glycerol phosphate dehydratase from M. tuberculosis. The position and environment of these derivatives in the enzyme active site are described. The results of these studies can be used to modify the triazole derivatives for the design of selective antituberculosis drugs.
Об авторах
Yu. Agapova
National Research Center “Kurchatov Institute”
Автор, ответственный за переписку.
Email: agapova.jk@gmail.com
Россия, Moscow, 123098
V. Timofeev
National Research Center “Kurchatov Institute”; Shubnikov Institute of Crystallography of the Federal Scientific Research Centre “Crystallography and Photonics,”Russian Academy of Sciences
Email: agapova.jk@gmail.com
Россия, Moscow, 123098; Moscow, 119333
A. Komolov
National Research Center “Kurchatov Institute”
Email: agapova.jk@gmail.com
Россия, Moscow, 123098
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