A complete model of the Plasmodium falciparum bifunctional enzyme dihydrofolate reductase-thymidylate synthase: a model to design new antimalarials

A complete model of the Plasmodium falciparum bifunctional enzyme dihydrofolate reductase-thymidylate synthase: a model to design new antimalarials

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 f...

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Main Authors: França Tanos C. C., Medeiros André L. R. de, Santos Edison C. P. dos, Santos-Filho Osvaldo A., Figueroa-Villar José D.
Format: Article
Language:English
Published: Sociedade Brasileira de Química 2004-01-01
Series:Journal of the Brazilian Chemical Society
Subjects:
malaria
homology modeling
DHFR-TS
optimized substrate transport
Plasmodium falciparum
Online Access:http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532004000300019
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spelling doaj-3689c865dfc6438ab6aa68f6434a9b2f2020-11-24T22:55:23ZengSociedade Brasileira de QuímicaJournal of the Brazilian Chemical Society0103-50532004-01-01153450454A complete model of the Plasmodium falciparum bifunctional enzyme dihydrofolate reductase-thymidylate synthase: a model to design new antimalarialsFrança Tanos C. C.Medeiros André L. R. deSantos Edison C. P. dosSantos-Filho Osvaldo A.Figueroa-Villar José D.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.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532004000300019malariahomology modelingDHFR-TSoptimized substrate transportPlasmodium falciparum
collection DOAJ
language English
format Article
sources DOAJ
author França Tanos C. C.
Medeiros André L. R. de
Santos Edison C. P. dos
Santos-Filho Osvaldo A.
Figueroa-Villar José D.
spellingShingle França Tanos C. C.
Medeiros André L. R. de
Santos Edison C. P. dos
Santos-Filho Osvaldo A.
Figueroa-Villar José D.
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
malaria
homology modeling
DHFR-TS
optimized substrate transport
Plasmodium falciparum
author_facet França Tanos C. C.
Medeiros André L. R. de
Santos Edison C. P. dos
Santos-Filho Osvaldo A.
Figueroa-Villar José D.
author_sort França Tanos C. C.
title A complete model of the Plasmodium falciparum bifunctional enzyme dihydrofolate reductase-thymidylate synthase: a model to design new antimalarials
title_short A complete model of the Plasmodium falciparum bifunctional enzyme dihydrofolate reductase-thymidylate synthase: a model to design new antimalarials
title_full A complete model of the Plasmodium falciparum bifunctional enzyme dihydrofolate reductase-thymidylate synthase: a model to design new antimalarials
title_fullStr A complete model of the Plasmodium falciparum bifunctional enzyme dihydrofolate reductase-thymidylate synthase: a model to design new antimalarials
title_full_unstemmed A complete model of the Plasmodium falciparum bifunctional enzyme dihydrofolate reductase-thymidylate synthase: a model to design new antimalarials
title_sort complete model of the plasmodium falciparum bifunctional enzyme dihydrofolate reductase-thymidylate synthase: a model to design new antimalarials
publisher Sociedade Brasileira de Química
series Journal of the Brazilian Chemical Society
issn 0103-5053
publishDate 2004-01-01
description 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.
topic malaria
homology modeling
DHFR-TS
optimized substrate transport
Plasmodium falciparum
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532004000300019
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