Crystal structure of human PNP complexed with hypoxanthine and sulfate ion
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
20/05/2014
20/05/2014
14/01/2005
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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 |