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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.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 309, n. 4, p. 917-922, 2003.
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.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.sourceWeb of Science
dc.subjectsynchrotron radiationpt
dc.subjectdrug designpt
dc.titleStructural basis for inhibition of human PNP by immucillin-Hen
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.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
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