Structures of human purine nucleoside phosphorylase complexed with inosine and ddI

Página do item simplificado
dc.contributor.authorCanduri, F.
dc.contributor.authordos Santos, D. M.
dc.contributor.authorSilva, R. G.
dc.contributor.authorMendes, M. A.
dc.contributor.authorBasso, L. A.
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.contributor.authorde Azevedo, W. F.
dc.contributor.authorSantos, D. S.
dc.contributor.institutionUniversidade Federal do Rio Grande do Sul (UFRGS)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionInstituto Butantan
dc.contributor.institutionPontificia Univ Catolica Rio Grande do Sul
dc.date.accessioned2014-05-20T13:54:24Z
dc.date.available2014-05-20T13:54:24Z
dc.date.issued2004-01-23
dc.description.abstractHuman 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 effect on B-cell function. PNP is highly specific for 6-oxopurine nucleosides and exhibits negligible activity for 6-aminopurine nucleosides. The catalytic efficiency for inosine is 350,000-fold greater than for adenosine. Adenine nucleosides and nucleotides are deaminated by adenosine deaminase and AMP deaminase to their corresponding inosine derivatives which, in turn, may be further degraded. Here we report the crystal structures of human PNP in complex with inosine and 2',3'-dideoxymosine, refined to 2.8 Angstrom resolution using synchrotron radiation. The present structures provide explanation for ligand binding, refine the purine-binding site, and can be used for future inhibitor design. (C) 2003 Elsevier B.V. All rights reserved.en
dc.description.affiliationUFRGS, Dept Biol Mol & Biotecnol, BR-91501970 Porto Alegre, RS, Brazil
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.affiliationUNESP, Inst Biosci, Dept Biol, CEIS,Lab Struct Biol & Zoochem, BR-13506900 Rio Claro, SP, Brazil
dc.description.affiliationPontificia Univ Catolica Rio Grande do 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.format.extent907-914
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2003.11.179
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 313, n. 4, p. 907-914, 2004.
dc.identifier.doi10.1016/j.bbrc.2003.11.179
dc.identifier.issn0006-291X
dc.identifier.lattes9424175688206545
dc.identifier.lattes2901888624506535
dc.identifier.urihttp://hdl.handle.net/11449/19449
dc.identifier.wosWOS:000187997700013
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.relation.ispartofjcr2.559
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectPNPpt
dc.subjectsynchrotron radiationpt
dc.subjectStructurept
dc.subjectdrug designpt
dc.titleStructures of human purine nucleoside phosphorylase complexed with inosine and ddIen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes9424175688206545
unesp.author.lattes2901888624506535
unesp.author.orcid0000-0002-2078-9286[4]
unesp.author.orcid0000-0002-7363-8211[6]
unesp.author.orcid0000-0002-1308-8190[3]
unesp.author.orcid0000-0003-0903-2407[5]
unesp.author.orcid0000-0003-4971-463X[8]
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

Arquivos

Licença do Pacote
Agora exibindo 1 - 1 de 1
Nenhuma Miniatura disponível
Nome:
license.txt
Tamanho:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descrição:

Coleções

Artigos - Física - IBILCE
Artigos - Biologia - IBRC