Structure of Plasmodium vivax dihydrofolate reductase determined by homology modeling and molecular dynamics refinement.

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Rastelli G, Pacchioni S, Parenti MD

Structure of Plasmodium vivax dihydrofolate reductase determined by homology modeling and molecular dynamics refinement.

Bioorg Med Chem Lett. 2003 Oct 6;13(19):3257-60.

PubMed ID

12951104 [ View in PubMed

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Abstract

The structure of Plasmodium vivax dihydrofolate reductase (PvDHFR), a potentially important target for antimalarial chemotherapy, was determined by means of homology modeling and molecular dynamics refinement. The structure proved to be consistent with DHFRs of known crystal structure. The comparison of the complexes of the antifolate inhibitor pyrimethamine bound at the active sites of PvDHFR and PfDHFR, the related enzyme from Plasmodium falciparum, prospected the possibility of using structure-based drug design to develop inhibitors that are effective against both malarial enzymes. This study constitutes a first step toward understanding of the antifolate-PvDHFR molecular interactions and possible rationalization of resistance in vivax malaria.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Pyrimethamine	Dihydrofolate reductase	Protein	Humans	Yes	Inhibitor	Details