Abstract
This work describes for the first time a model of Purine Nucleoside Phosphorylase from Listeria monocytogenes (LmPNP). We modeled the complexes of LmPNP with ligands in order to determine the structural basis for specificity. Comparative analysis of the model of LmPNP allowed identification of structural features responsible for ligand affinities.
Keywords: Purine Nucleoside Phosphorylase, molecular modeling, bioinformatics, drug design, Listeria monocytogenes
Protein & Peptide Letters
Title: Structural Bioinformatics Study of PNP from Listeria monocytogenes
Volume: 15 Issue: 8
Author(s): L. F.S.M. Timmers, R. A. Caceres, L. A. Basso, D. S. Santos and W. F. De Azevedo, Jr.
Affiliation:
Keywords: Purine Nucleoside Phosphorylase, molecular modeling, bioinformatics, drug design, Listeria monocytogenes
Abstract: This work describes for the first time a model of Purine Nucleoside Phosphorylase from Listeria monocytogenes (LmPNP). We modeled the complexes of LmPNP with ligands in order to determine the structural basis for specificity. Comparative analysis of the model of LmPNP allowed identification of structural features responsible for ligand affinities.
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Cite this article as:
Timmers F.S.M. L., Caceres A. R., Basso A. L., Santos S. D. and De Azevedo, Jr. F. W., Structural Bioinformatics Study of PNP from Listeria monocytogenes, Protein & Peptide Letters 2008; 15 (8) . https://dx.doi.org/10.2174/092986608785203728
DOI https://dx.doi.org/10.2174/092986608785203728 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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