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：5
页码：3740
DOI：10.15680/IJIRSET.2015.0405128
出版社：S&S Publications
摘要：In this study, we analyzed and compared the interactions of an antibiotic drug, trimethoprim, with nativeand mutant human Dihydrofolate Reductase DHFR structures by computational methods. We observed that, Ile7,Glu30, Leu22, Val115, Pro61, Phe179 and Tyr182 of native DHFR play an important role in interacting withtrimethoprim. Ile7, Glu30, Val112, Trp113, Ile114 and Leu133 of mutant DHFRare identified as key residues ininteracting with trimethoprim. This study would help in modifying the structure of trimethoprim for improved affinityof the drug towards the native and mutant structures of human dihydrofolate reductase.
