The interactions of dihydrofolate with M. tuberculosis dihydrofolate reductase
- Resource Type
- Conference
- Authors
- Sittikornpaiboon, Pimonluck; Toochinda, Pisanu; Lawtrakul, Luckhana
- Source
- 2016 Second Asian Conference on Defence Technology (ACDT) Defence Technology (ACDT), 2016 Second Asian Conference on. :183-186 Jan, 2016
- Subject
- Aerospace
Communication, Networking and Broadcast Technologies
Computing and Processing
General Topics for Engineers
Nuclear Engineering
Robotics and Control Systems
Signal Processing and Analysis
Biochemistry
Nickel
Minimization
Nanotechnology
DHFR
dihydrofolate reductase
mycobacterium tuberculosis
dihydrofolate
molecular dynamics simulation
- Language
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.