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Literature summary for 1.5.1.3 extracted from

  • Maitarad, P.; Saparpakorn, P.; Hannongbua, S.; Kamchonwongpaisan, S.; Tarnchompoo, B.; Yuthavong, Y.
    Particular interaction between pyrimethamine derivatives and quadruple mutant type dihydrofolate reductase of Plasmodium falciparum: CoMFA and quantum chemical calculations studies (2008), J. Enzyme Inhib. Med. Chem., 24, 471-479.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
CoMFA and quantum chemical calculations studies on pyrimethamine derivatives active against quadruple mutant N5I/C59R/S108N/I164L. Residue N108 is the cause of pyrimethamine resistance with the highest repulsive interaction energy Plasmodium falciparum

Protein Variants

Protein Variants Comment Organism
N5I/C59R/S108N/I164L naturally occuring mutant. Residue N108 is the cause of pyrimethamine resistance with the highest repulsive interaction energy Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
pyrimethamine CoMFA and quantum chemical calculations studies on pyrimethamine derivatives active against quadruple mutant N5I/C59R/S108N/I164L. Residue N108 is the cause of pyrimethamine resistance with the highest repusive interaction energy Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum P13922
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