Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10772059 | Biochemical and Biophysical Research Communications | 2005 | 4 Pages |
Abstract
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 2.6Â Ã
resolution. The intermolecular interaction between ligand and PNP is discussed.
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Authors
Fernanda Canduri, Valmir Fadel, Marcio VinÃcius Bertacine Dias, Luiz Augusto Basso, Mário Sérgio Palma, Diógenes Santiago Santos, Walter Filgueira Jr.,