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
- Universidade Federal do Rio Grande do Sul (UFRGS)
- Universidade Estadual Paulista (UNESP)
- Instituto Butantan
- Pontifícia Universidade Católica do Rio Grande do Sul (PUCRS)
- 0006-291X
- 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.
- 14-Jan-2005
- Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 326, n. 2, p. 335-338, 2005.
- 335-338
- Elsevier B.V.
- PNP
- synchrotron radiation
- Structure
- drug design
- hypoxanthine
- http://dx.doi.org/10.1016/j.bbrc.2004.11.038
- Acesso restrito
- outro
- http://repositorio.unesp.br/handle/11449/19455
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.