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

Tanos C. C. França¹  André L. R. De Medeiros¹  Edison C. P. Dos Santos¹  Osvaldo A. Santos-filho¹  José D. Figueroa-villar¹ 

[1] ,Instituto Militar de Engenharia Departamento de Química Rio de Janeiro RJ ,Brasil

关键词: malaria;    homology modeling;    DHFR-TS;    optimized substrate transport;    Plasmodium falciparum;   

DOI  :  10.1590/S0103-50532004000300019

来源: SciELO

【 摘 要 】

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.

【 授权许可】

CC BY   
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