The Interactions of Dihydrofolate with M. tuberculosis Dihydrofolate Reductase

摘要

The molecular dynamics (MD) simulation was used to determine the interactions and binding affinities of Mycobacterium tuberculosis dihydrofolate reductase (mtbDHFR) in complex with dihydrofolate (DHF), which is the natural substrate of the enzyme. The MD simulation approach can predict the ternary complexes of mtbDHFR with NADPH and DHF in the present of solvent. Our predicted structure can use to study the interaction of the DHF to mtbDHFR and provides insight into the important interactions of mtbDHFR with DHF, which lead to the design of effective agents against mtbDHFR in the future.