Structure of human PNP complexed with ligands


Autoria(s): Canduri, F.; Silva, R. G.; dos Santos, D. M.; Palma, Mario Sergio; Basso, L. A.; Santos, D. S.; de Azevedo, W. F.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

01/07/2005

Resumo

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.

Formato

856-862

Identificador

http://dx.doi.org/10.1107/S0907444905005421

Acta Crystallographica Section D-biological Crystallography. Oxford: Blackwell Publishing, v. 61, p. 856-862, 2005.

0907-4449

http://hdl.handle.net/11449/19553

10.1107/S0907444905005421

WOS:000230113000003

Idioma(s)

eng

Publicador

Blackwell Publishing

Relação

Acta Crystallographica Section D: Biological Crystallography

Direitos

closedAccess

Tipo

info:eu-repo/semantics/article