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Crystal structure of human PNP complexed with hypoxanthine and sulfate ion |
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| Authors: | Canduri Fernanda Fadel Valmir Dias Marcio Vinícius Bertacine Basso Luiz Augusto Palma Mário Sérgio Santos Diógenes Santiago de Azevedo Walter Filgueira |
| Institution: | a Programa de Pós-graduação em Biofísica Molecular, Departamento de Física, UNESP, São José do Rio Preto, SP 15054-000, Brazil b Center for Applied Toxinology, Instituto Butantan, São Paulo, SP 05503-900, Brazil c Rede Brasileira de Pesquisas em Tuberculose, Departamento de Biologia Molecular e Biotecnologia, UFRGS, Porto Alegre, RS 91501-970, Brazil d Laboratory of Structural Biology and Zoochemistry-CEIS/Department of Biology, Institute of Biosciences, UNESP, Rio Claro, SP 13506-900, Brazil e Centro de Pesquisas em Biologia Molecular e Funcional, Instituto de Pesquisas Biomédicas, PUCRS, Porto Alegre, RS, 90619-900, Brazil |
| 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 2.6A resolution. The intermolecular interaction between ligand and PNP is discussed. |
| Keywords: | PNP Synchrotron radiation Structure Drug design Hypoxanthine |
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