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dc.contributor.authorde Azevedo, W. F.
dc.contributor.authorCanduri, F.
dc.contributor.authordos Santos, D. M.
dc.contributor.authorPereira, J. H.
dc.contributor.authorDias, MVB
dc.contributor.authorSilva, R. G.
dc.contributor.authorMendes, M. A.
dc.contributor.authorBasso, L. A.
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.contributor.authorSantosce, D. S.
dc.date.accessioned2014-05-20T13:55:37Z
dc.date.available2014-05-20T13:55:37Z
dc.date.issued2003-10-03
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2003.08.094
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 309, n. 4, p. 917-922, 2003.
dc.identifier.issn0006-291X
dc.identifier.urihttp://hdl.handle.net/11449/19907
dc.description.abstractPurine nucleoside phosphorylase (PNP) catalyzes the phosphorolysis of the N-ribosidic bonds of purine nucleosides and deoxynucleosides. PNP is a target for inhibitor development aiming at T-cell immune response modulation. This work reports on the crystallographic study of the complex of human PNP-immucillin-H (HsPNP-ImmH) solved at 2.6 Angstrom resolution using synchrotron radiation. Immucillin-H (ImmH) inhibits the growth of malignant T-cell lines in the presence of deoxyguanosine without affecting non-T-cell tumor lines. ImmH inhibits activated normal human T cells after antigenic stimulation in vitro. These biological effects of ImmH suggest that this agent may have utility in the treatment of certain human diseases characterized by abnormal T-cell growth or activation. This is the first structural report of human PNP complexed with immucillin-H. The comparison of the complex HsPNP-ImmH with recent crystallographic structures of human PNP explains the high specificity of immucillin-H for human PNP. (C) 2003 Elsevier B.V. All rights reserved.en
dc.format.extent917-922
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.sourceWeb of Science
dc.subjectPNPpt
dc.subjectsynchrotron radiationpt
dc.subjectStructurept
dc.subjectimmucillin-Hpt
dc.subjectdrug designpt
dc.titleStructural basis for inhibition of human PNP by immucillin-Hen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionInstituto Butantan
dc.contributor.institutionUniversidade Federal do Rio Grande do Sul (UFRGS)
dc.contributor.institutionPontificia Univ Catolica Rio Grande Sul
dc.description.affiliationUNESP, 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.affiliationUFRGS, Dept Biol Mol & Biotecnol, Rede Brasileira Pesquisas TB, BR-91501970 Porto Alegre, RS, Brazil
dc.description.affiliationUNESP, Inst Biosci, Dept Biol, CEIS,Lab Struct Biol & Zoochem, BR-13506900 Rio Claro, SP, Brazil
dc.description.affiliationPontificia Univ Catolica Rio Grande Sul, Inst Pesquisas Biomed, Fac Farm, Porto Alegre, RS, Brazil
dc.description.affiliationUnespUNESP, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUNESP, Inst Biosci, Dept Biol, CEIS,Lab Struct Biol & Zoochem, BR-13506900 Rio Claro, SP, Brazil
dc.identifier.doi10.1016/j.bbrc.2003.08.094
dc.identifier.wosWOS:000185774300032
dc.rights.accessRightsAcesso restrito
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Rio Claropt
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt
dc.identifier.lattes9424175688206545
unesp.author.lattes9424175688206545
unesp.author.orcid0000-0002-7363-8211[9]
unesp.author.orcid0000-0002-5312-0191[5]
unesp.author.orcid0000-0002-2078-9286[7]
unesp.author.orcid0000-0003-0903-2407[8]
unesp.author.orcid0000-0002-1308-8190[6]
dc.relation.ispartofjcr2.559
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