Literature DB >> 21875154

Molecular modeling studies of Yersinia pestis dihydrofolate reductase.

Aline A Oliveira1, Magdalena N Rennó, César A de Matos, Morena D Bertuzzi, Teodorico C Ramalho, Carlos A M Fraga, Tanos C C França.   

Abstract

Considering the risk represented by plague today as a potential biological warfare agent, we propose cytosolic Yersinia pestis dihydrofolate reductase (YpDHFR) as a new target to the design of selective plague chemotherapy. This enzyme has a low homology with the human enzyme and its crystallographic structure has been recently deposited in the Protein Data Bank (PDB). Comparisons of the docking energies and molecular dynamic behaviors of five known DHFR inhibitors inside a 3D model of YpDHFR (adapted from the crystallographic structure) and human DHFR (HssDHFR), revealed new potential interactions and suggested insights into the design of more potent HssDHFR inhibitors as well as selective inhibitors for YpDHFR.

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Year:  2011        PMID: 21875154     DOI: 10.1080/07391102.2011.10507390

Source DB:  PubMed          Journal:  J Biomol Struct Dyn        ISSN: 0739-1102


  2 in total

1.  Insight into the molecular mechanism about lowered dihydrofolate binding affinity to dihydrofolate reductase-like 1 (DHFRL1).

Authors:  Jian Gao; Wei Cui; Yuguo Du; Mingjuan Ji
Journal:  J Mol Model       Date:  2013-10-12       Impact factor: 1.810

2.  Analyses of the Binding between Water Soluble C60 Derivatives and Potential Drug Targets through a Molecular Docking Approach.

Authors:  Muhammad Junaid; Eman Abdullah Almuqri; Junjun Liu; Houjin Zhang
Journal:  PLoS One       Date:  2016-02-01       Impact factor: 3.240

  2 in total

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