Structure of human PNP complexed with ligands
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
20/05/2014
20/05/2014
01/07/2005
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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 |