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Solution structures and dynamics of the dihydrofolate reductase complexes with anti-bacterial drug trimethoprimтезисы доклада
- Авторы: Kovalevskaya N.V., Smurnyy Y.D., Birdsall B., Feeney J., Polshakov V.I.
- Сборник: The proceedings of international symposium on Computational Methods in Pharmacology And Toxicology Integrating Internet Resources
- Тезисы
- Год издания: 2007
- Место издания: Moscow, Russia
- Первая страница: 112
- Последняя страница: 112
- Аннотация: Dihydrofolate reductase (DHFR) catalyses the NADPH-dependent reduction of folate and dihydrofolate to tetrahydrofolate. Since the latter is an important cofactor in the biosynthesis of purines and amino acids, DHFR has proved to be an excellent target for antifolate drugs that act by inhibiting the enzyme in parasitic or malignant cells. The effectiveness of antibacterial drug trimethoprim (TMP) is due to its significantly increased ability of the binding to the bacterial enzyme compared with the vertebrate form. In order to explore the origins of the selectivity of TMP binding to DHFR, information on the structure and dynamics of the complexes of human and Lactobacillus casei forms of enzyme with TMP and/or cofactor NADPH is obtained using the NMR spectroscopy methods and molecular dynamics calculations.
- Добавил в систему: Польшаков Владимир Иванович