1m73
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CRYSTAL STRUCTURE OF HUMAN PNP AT 2.3A RESOLUTION
OverviewOverview
Purine nucleoside phosphorylase (PNP) catalyzes the phosphorolysis of the, N-ribosidic bonds of purine nucleosides and deoxynucleosides. In human, PNP is the only route for degradation of deoxyguanosine and genetic, deficiency of this enzyme leads to profound T-cell mediated, immunosuppression. PNP is therefore a target for inhibitor development, aiming at T-cell immune response modulation and its low resolution, structure has been used for drug design. Here we report the structure of, human PNP solved to 2.3A resolution using synchrotron radiation and, cryocrystallographic techniques. This structure allowed a more precise, analysis of the active site, generating a more reliable model for, substrate binding. The higher resolution data allowed the identification, of water molecules in the active site, which suggests binding partners for, potential ligands. Furthermore, the present structure may be used in the, new structure-based design of PNP inhibitors.
DiseaseDisease
Known diseases associated with this structure: Neutral lipid storage disease with myopathy OMIM:[609059], Nucleoside phosphorylase deficiency, immunodeficiency due to OMIM:[164050]
About this StructureAbout this Structure
1M73 is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Active as Purine-nucleoside phosphorylase, with EC number 2.4.2.1 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human purine nucleoside phosphorylase at 2.3A resolution., de Azevedo WF Jr, Canduri F, dos Santos DM, Silva RG, de Oliveira JS, de Carvalho LP, Basso LA, Mendes MA, Palma MS, Santos DS, Biochem Biophys Res Commun. 2003 Aug 29;308(3):545-52. PMID:12914785
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