Crystal structure of human PNP complexed with hypoxanthine and sulfate ion

Purine nucleoside phosphorylase (PNP) is a ubiquitous enzyme, which plays a key role in the purine salvage pathway, and PNP deficiency in humans leads to an impairment of T-cell function, usually with no apparent effects on B-cell function. Human PNP has been submitted to intensive structure-based d...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2005-01, Vol.326 (2), p.335-338
Main Authors: Canduri, Fernanda, Fadel, Valmir, Dias, Marcio Vinícius Bertacine, Basso, Luiz Augusto, Palma, Mário Sérgio, Santos, Diógenes Santiago, de Azevedo, Walter Filgueira
Format: Article
Language:English
Subjects:
Crystallography, X-Ray
Drug design
Humans
Hypoxanthine
Hypoxanthine - chemistry
Hypoxanthine - metabolism
Ions - chemistry
Ions - metabolism
Ligands
Models, Molecular
Molecular Structure
PNP
Protein Conformation
Purine-Nucleoside Phosphorylase - chemistry
Purine-Nucleoside Phosphorylase - metabolism
Structure
Sulfates - chemistry
Sulfates - metabolism
Synchrotron radiation
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Summary:Purine nucleoside phosphorylase (PNP) is a ubiquitous enzyme, which plays a key role in the purine salvage pathway, and PNP deficiency in humans leads to an impairment of T-cell function, usually with no apparent effects on B-cell function. Human PNP has been submitted to intensive structure-based design of inhibitors, most of them using low-resolution structures of human PNP. Here we report the crystal structure of human PNP in complex with hypoxanthine, refined to 2.6 Å resolution. The intermolecular interaction between ligand and PNP is discussed.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2004.11.038