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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/19455
Title: 
Crystal structure of human PNP complexed with hypoxanthine and sulfate ion
Author(s): 
Institution: 
  • Universidade Federal do Rio Grande do Sul (UFRGS)
  • Universidade Estadual Paulista (UNESP)
  • Instituto Butantan
  • Pontifícia Universidade Católica do Rio Grande do Sul (PUCRS)
ISSN: 
0006-291X
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 2.6 Angstrom resolution. The intermolecular interaction between ligand and PNP is discussed. (C) 2004 Elsevier B.V. All rights reserved.
Issue Date: 
14-Jan-2005
Citation: 
Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 326, n. 2, p. 335-338, 2005.
Time Duration: 
335-338
Publisher: 
Elsevier B.V.
Keywords: 
  • PNP
  • synchrotron radiation
  • Structure
  • drug design
  • hypoxanthine
Source: 
http://dx.doi.org/10.1016/j.bbrc.2004.11.038
URI: 
Access Rights: 
Acesso restrito
Type: 
outro
Source:
http://repositorio.unesp.br/handle/11449/19455
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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