Artículos de revistas
Structure of human PNP complexed with ligands
Fecha
2005-07-01Registro en:
Acta Crystallographica Section D-biological Crystallography. Oxford: Blackwell Publishing, v. 61, p. 856-862, 2005.
0907-4449
10.1107/S0907444905005421
WOS:000230113000003
9424175688206545
2901888624506535
Autor
Universidade Federal do Rio Grande do Sul (UFRGS)
Universidade Estadual Paulista (Unesp)
Instituto Butantan
Pontifícia Universidade Católica do Rio Grande do Sul (PUCRS)
Institución
Resumen
Purine nucleoside phosphorylase (PNP) is a key enzyme in the purine-salvage pathway, which allows cells to utilize preformed bases and nucleosides in order to synthesize nucleotides. PNP is specific for purine nucleosides in the beta-configuration and exhibits a strong preference for purines containing a 6-keto group and ribosyl-containing nucleosides relative to the corresponding analogues. PNP was crystallized in complex with ligands and data collection was performed using synchrotron radiation. This work reports the structure of human PNP in complex with guanosine (at 2.80 angstrom resolution), 3' deoxyguanosine (at 2.86 angstrom resolution) and 8-azaguanine (at 2.85 angstrom resolution). These structures were compared with the PNP-guanine, PNP-inosine and PNP-immucillin-H complexes solved previously.