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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/19455
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dc.contributor.authorCanduri, F.-
dc.contributor.authorFadel, V-
dc.contributor.authorDias, MVB-
dc.contributor.authorBasso, L. A.-
dc.contributor.authorPalma, Mario Sergio-
dc.contributor.authorSantos, D. S.-
dc.contributor.authorde Azevedo, W. F.-
dc.date.accessioned2014-05-20T13:54:25Z-
dc.date.accessioned2016-10-25T17:04:34Z-
dc.date.available2014-05-20T13:54:25Z-
dc.date.available2016-10-25T17:04:34Z-
dc.date.issued2005-01-14-
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2004.11.038-
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 326, n. 2, p. 335-338, 2005.-
dc.identifier.issn0006-291X-
dc.identifier.urihttp://hdl.handle.net/11449/19455-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/19455-
dc.description.abstractPurine 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.en
dc.format.extent335-338-
dc.language.isoeng-
dc.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjectPNPpt
dc.subjectsynchrotron radiationpt
dc.subjectStructurept
dc.subjectdrug designpt
dc.subjecthypoxanthinept
dc.titleCrystal structure of human PNP complexed with hypoxanthine and sulfate ionen
dc.typeoutro-
dc.contributor.institutionUniversidade Federal do Rio Grande do Sul (UFRGS)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionInstituto Butantan-
dc.contributor.institutionPontifícia Universidade Católica do Rio Grande do Sul (PUCRS)-
dc.description.affiliationUFRGS, Dept Mol Biol & Biotechnol, BR-91501970 Porto Alegre, RS, Brazil-
dc.description.affiliationUNESP, Programa Posgraduacao Biofis Mol, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationInst Butantan, Ctr Appl Toxinol, BR-05503900 São Paulo, Brazil-
dc.description.affiliationUNESP, Lab Struct Biol & Zoochem, CEIS, Dept Biol,Inst Biosci, BR-13506900 Rio Claro, SP, Brazil-
dc.description.affiliationPUCRS, Ctr Pesquisas Biol Mol & Func, Inst Pesquisas Biomed, BR-90619900 Porto Alegre, RS, Brazil-
dc.description.affiliationUnespUNESP, Programa Posgraduacao Biofis Mol, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUnespUNESP, Lab Struct Biol & Zoochem, CEIS, Dept Biol,Inst Biosci, BR-13506900 Rio Claro, SP, Brazil-
dc.identifier.doi10.1016/j.bbrc.2004.11.038-
dc.identifier.wosWOS:000225997300011-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofBiochemical and Biophysical Research Communications-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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