Structural bioinformatics study of PNP from Listeria monocytogenes.
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.
Faculdade de Biociências, Pontifícia Universidade Catílica do Rio Grande do Sul, Porto Alegre - RS, Brazil.
L F S M
LF
Timmers
R A
RA
Caceres
L A
LA
Basso
D S
DS
Santos
W F
WF
De Azevedo
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000494:pharmacology / Q000627:therapeutic use; D001051:Apoenzymes / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D019295:Computational Biology; D015195:Drug Design; D006801:Humans; D008024:Ligands; D008089:Listeria monocytogenes / Q000187:drug effects / Q000201:enzymology*; D008088:Listeriosis / Q000188:drug therapy; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D011683:Purine-Nucleoside Phosphorylase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity
D000900:Anti-Bacterial Agents; D001051:Apoenzymes; D008024:Ligands; D011683:Purine-Nucleoside Phosphorylase