Crystal structure of human PNP complexed with hypoxanthine and sulfate ion

Autor(es)

Canduri, Fernanda ; Fadel, Valmir ; Dias, Marcio Vinícius Bertacine ^[3] ; Basso, Luiz Augusto ; Palma, Mário Sérgio ; Santos, Diógenes Santiago ; Azevedo Júnior, Walter Filgueira de

• Tipo de documento: Artigo Científico
• Fonte: Biochemical and Biophysical Research Communications; v. 326, n. 2, p. 335-338, Jan. 2005.
• Área do conhecimento: Ciências Biológicas - Biofísica
• Assunto(s): Biofísica Inibidores enzimáticos

Resumo

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 resolution. The intermolecular interaction between ligand and PNP is discussed. (AU)

• Processo FAPESP: 01/07532-0 - Structural genomics of cyclin dependent kinases and plant defensive proteinases and their natural inhibitors
• Beneficiário: Walter Filgueira de Azevedo Junior
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 04/00217-0 - Estudo estrutural de proteinas alvos para desenho de drogas contra tuberculose.
• Beneficiário: Walter Filgueira de Azevedo Junior
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 02/04383-7 - Estudo estrutural das enzimas da via metabólica do ácido chiquímico
• Beneficiário: Walter Filgueira de Azevedo Junior
• Modalidade de apoio: Auxílio à Pesquisa - Regular