Crystal structure of human PNP complexed with hypoxanthine and sulfate ion
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Data
2005-01-14
Autores
Canduri, F.
Fadel, V
Dias, MVB
Basso, L. A.
Palma, Mario Sergio [UNESP]
Santos, D. S.
de Azevedo, W. F.
Título da Revista
ISSN da Revista
Título de Volume
Editor
Elsevier B.V.
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 Angstrom resolution. The intermolecular interaction between ligand and PNP is discussed. (C) 2004 Elsevier B.V. All rights reserved.
Descrição
Palavras-chave
PNP, synchrotron radiation, Structure, drug design, hypoxanthine
Como citar
Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 326, n. 2, p. 335-338, 2005.