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Research Article Open Access
In this study, we analyzed and compared the interactions of an antibiotic drug, trimethoprim, with native and 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 with trimethoprim. Ile7, Glu30, Val112, Trp113, Ile114 and Leu133 of mutant DHFRare identified as key residues in interacting with trimethoprim. This study would help in modifying the structure of trimethoprim for improved affinity of the drug towards the native and mutant structures of human dihydrofolate reductase.
Antibiotic drug, Trimethoprim, Dihydrofolate reductase, Mutant, Enzymes