%0 Journal Article
%T A complete model of the Plasmodium falciparum bifunctional enzyme dihydrofolate reductase-thymidylate synthase: a model to design new antimalarials
%A Fran£¿a
%A Tanos C. C.
%A Medeiros
%A Andr¨¦ L. R. de
%A Santos
%A Edison C. P. dos
%A Santos-Filho
%A Osvaldo A.
%A Figueroa-Villar
%A Jos¨¦ D.
%J Journal of the Brazilian Chemical Society
%D 2004
%I Sociedade Brasileira de Qu¨ªmica, SBQ
%R 10.1590/S0103-50532004000300019
%X 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.
%K malaria
%K homology modeling
%K dhfr-ts
%K optimized substrate transport
%K plasmodium falciparum.
%U http://www.scielo.br/scielo.php?script=sci_abstract&pid=S0103-50532004000300019&lng=en&nrm=iso&tlng=en