期刊名称：International Journal of Innovative Research in Science, Engineering and Technology
印刷版ISSN：2347-6710
电子版ISSN：2319-8753
出版年度：2015
卷号：4
期号：9
页码：9202
DOI：10.15680/IJIRSET.2015.0409135
出版社：S&S Publications
摘要：Dihydrofolate reductase (DHFR) is an important enzyme in the cell and is the target for antifolate drugssuch as methotrexate, pyrimethamine and trimethoprim. In this study, we compared the binding interactions oftrimethoprim with native and mutant structure of DHFR by computational methods. We generated four mutantstructures of DHFR by using UCSF chimera. Binding energies of trimethoprim with native and mutant structures ofDHFR were computed by using Autodock. Finally, one mutant structure (1YHO_Q35I) which has been generated bycomputational methods, has shown a high affinity binding affinity towards the trimethoprim the native other mutantstructures.
