Structure of human PNP complexed with ligands
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Data
2005-07-01
Autores
Canduri, F.
Silva, R. G.
dos Santos, D. M.
Palma, Mario Sergio [UNESP]
Basso, L. A.
Santos, D. S.
de Azevedo, W. F.
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Blackwell Publishing
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.
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Acta Crystallographica Section D-biological Crystallography. Oxford: Blackwell Publishing, v. 61, p. 856-862, 2005.