Crystal structure of human PNP complexed with hypoxanthine and sulfate ion


Autoria(s): Canduri, F.; Fadel, V; Dias, MVB; Basso, L. A.; Palma, Mario Sergio; Santos, D. S.; de Azevedo, W. F.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

14/01/2005

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.

Formato

335-338

Identificador

http://dx.doi.org/10.1016/j.bbrc.2004.11.038

Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 326, n. 2, p. 335-338, 2005.

0006-291X

http://hdl.handle.net/11449/19455

10.1016/j.bbrc.2004.11.038

WOS:000225997300011

Idioma(s)

eng

Publicador

Elsevier B.V.

Relação

Biochemical and Biophysical Research Communications

Direitos

closedAccess

Palavras-Chave #PNP #synchrotron radiation #Structure #drug design #hypoxanthine
Tipo

info:eu-repo/semantics/article