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dc.contributor.authorNolasco, D. O.-
dc.contributor.authorCanduri, F.-
dc.contributor.authorPereira, J. H.-
dc.contributor.authorCortinoz, JR-
dc.contributor.authorPalma, Mario Sergio-
dc.contributor.authorOliveira, J. S.-
dc.contributor.authorBasso, L. A.-
dc.contributor.authorde Azevedo, W. F.-
dc.contributor.authorSantos, D. S.-
dc.date.accessioned2014-05-20T13:54:20Z-
dc.date.accessioned2016-10-25T17:04:30Z-
dc.date.available2014-05-20T13:54:20Z-
dc.date.available2016-10-25T17:04:30Z-
dc.date.issued2004-11-12-
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2004.09.137-
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 324, n. 2, p. 789-794, 2004.-
dc.identifier.issn0006-291X-
dc.identifier.urihttp://hdl.handle.net/11449/19413-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/19413-
dc.description.abstractEven being a bacterial purine nucleoside phosphorylase (PNP), which normally shows hexameric folding, the Mycobacterium tuberculosis PNP (MtPNP) resembles the mammalian trimeric structure. The crystal structure of the MtPNP apoenzyme was solved at 1.9 Angstrom resolution. The present work describes the first structure of MtPNP in complex with phosphate. In order to develop new insights into the rational drug design, conformational changes were profoundly analyzed and discussed. Comparisons over the binding sites were specially studied to improve the discussion about the selectivity of potential new drugs. (C) 2004 Elsevier B.V. All rights reserved.en
dc.format.extent789-794-
dc.language.isoeng-
dc.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjecttuberculosispt
dc.subjectPNPpt
dc.subjectCrystallographypt
dc.subjectapoenzymept
dc.subjectselectivitypt
dc.titleCrystallographic structure of PNP from Mycobacterium tuberculosis at 1.9 angstrom resolutionen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionPontifícia Universidade Católica do Rio Grande do Sul (PUCRS)-
dc.description.affiliationUNESP, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUNESP, Programa Posgrad Biofis Mol, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUNESP, Inst Biosci, Dept Biol, Lab Struct Biol & Zoochem,CEIS, BR-13506900 Rio Claro, SP, Brazil-
dc.description.affiliationPUCRS, Ctr Pesquisa Biol Mol & Funct, Rede Brasileira Pesquisa TB, BR-90619900 Porto Alegre, RS, Brazil-
dc.description.affiliationUnespUNESP, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUnespUNESP, Programa Posgrad Biofis Mol, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUnespUNESP, Inst Biosci, Dept Biol, Lab Struct Biol & Zoochem,CEIS, BR-13506900 Rio Claro, SP, Brazil-
dc.identifier.doi10.1016/j.bbrc.2004.09.137-
dc.identifier.wosWOS:000224794000046-
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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