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. 2020 Feb 18;25(4):904. doi: 10.3390/molecules25040904

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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(A) Illustration of the P. falciparum thymidylate synthase domain of dihydrofolate reductase (DHFR-TS) dimeric assembly: The structure was generated using homology modeling technique. P. falciparum Protein Data Bank (PDB) ID: 3QGT was used as a template. Color key: blue: DHFR domain, red: DHFR-TS junction, grey: TS domain. (B) Zoomed in image of the DHFR domain complexed with nicotinamide adenine dinucleotide phosphate (NADPH) cofactor and pyrimethamine. (C) Structural mapping of pyrimethamine-resistant mutations assessed in this study. (D) Wireframe representation of the structure of pyrimethamine.