Molecular modeling and dynamics studies of purine nucleoside phosphorylase from Bacteroides fragilis |
| |
Authors: | Ivani Pauli Luis Fernando Saraiva Macedo Timmers Rafael Andrade Caceres Luiz Augusto Basso Diógenes Santiago Santos Walter Filgueira de Azevedo Jr |
| |
Institution: | 1. Laboratório de Bioquímica Estrutural, Faculdade de Biociências, Pontifícia Universidade Católica do Rio Grande do Sul, Porto Alegre, RS, Brazil 2. Programa de Pós-Gradua??o em Medicina e Ciências da Saúde, Pontifícia Universidade Católica do Rio Grande do Sul, Porto Alegre, RS, Brazil 3. Instituto de Pesquisas Biomédicas, Centro de Pesquisas em Biologia Molecular e Funcional, Pontifícia Universidade Católica do Rio Grande do Sul, Porto Alegre, RS, Brazil
|
| |
Abstract: | Purine nucleoside phosphorylase (PNP) catalyzes the reversible phosphorolysis of N-ribosidic bonds of purine nucleosides and deoxynucleosides, except adenosine, to generate ribose 1-phosphate and the purine
base. This work describes for the first time a structural model of PNP from Bacteroides fragilis (Bf). We modeled the complexes of BfPNP with six different ligands in order to determine the structural basis for specificity of these ligands against BfPNP. Comparative analysis of the model of BfPNP and the structure of HsPNP allowed identification of structural features responsible for differences in the computationally determined ligand affinities.
The molecular dynamics (MD) simulation was assessed to evaluate the overall stability of the BfPNP model. The superposition of the final onto the initial minimized structure shows that there are no major conformational
changes from the initial model, which is consistent with the relatively low root mean square deviation (RMSD). The results
indicate that the structure of the model was stable during MD, and does not exhibit loosely structured loop regions or domain
terminals. |
| |
Keywords: | Bacteroides fragilis Bioinformatics Drug-design Molecular dynamics Molecular modeling |
本文献已被 SpringerLink 等数据库收录! |
|