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Crystal structure of human PNP complexed with hypoxanthine and sulfate ion.
Canduri, Fernanda; Fadel, Valmir; Dias, Marcio Vinícius Bertacine; Basso, Luiz Augusto; Palma, Mário Sérgio; Santos, Diógenes Santiago; de Azevedo, Walter Filgueira.
Afiliación
  • Canduri F; Programa de Pós-graduação em Biofísica Molecular, Departamento de Física, UNESP, São José do Rio Preto, SP 15054-000, Brazil.
Biochem Biophys Res Commun ; 326(2): 335-8, 2005 Jan 14.
Article en En | MEDLINE | ID: mdl-15582582
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.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sulfatos / Purina-Nucleósido Fosforilasa / Hipoxantina Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 2005 Tipo del documento: Article País de afiliación: Brasil
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sulfatos / Purina-Nucleósido Fosforilasa / Hipoxantina Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 2005 Tipo del documento: Article País de afiliación: Brasil
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