Abstract
We propose a theoretical model for pfDHFR-TS, which includes the 55 aminoacid residues ignored in the crystallographic model. The electrostatic potential calculation on the model surface revealed a continuous positive potential region between the two active sites, suggesting an optimized - mechanism for dihydrofolate transport.
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França, T. C. C., De Medeiros, A. L. R., Dos Santos, E. C. P., Santos-Filho, O. A., & Figueroa-Villar, J. D. (2004). A complete model of the Plasmodium falciparum bifunctional enzyme dihydrofolate reductase-thymidylate synthase. A model to design new antimalarials. Journal of the Brazilian Chemical Society, 15(3), 450–454. https://doi.org/10.1590/S0103-50532004000300019
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