Crystal structure of human purine nucleoside phosphorylase at 2.3 angstrom resolution

Página do item simplificado
dc.contributor.authorde Azevedo, W. F.
dc.contributor.authorCanduri, F.
dc.contributor.authordos Santos, D. M.
dc.contributor.authorSilva, R. G.
dc.contributor.authorde Oliveira, J. S.
dc.contributor.authorde Carvalho, LPS
dc.contributor.authorBasso, L. A.
dc.contributor.authorMendes, M. A.
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.contributor.authorSantos, D. S.
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 do Sul
dc.date.accessioned2014-05-20T13:54:37Z
dc.date.available2014-05-20T13:54:37Z
dc.date.issued2003-08-29
dc.description.abstractPurine nucleoside phosphorylase (PNP) catalyzes the phosphorolysis of the N-ribosidic bonds of purine nucleosides and deoxynucleosides. In human, PNP is the only route for degradation of deoxyguanosine and genetic deficiency of this enzyme leads to profound T-cell mediated immunosuppression. PNP is therefore a target for inhibitor development aiming at T-cell immune response modulation and its low resolution structure has been used for drug design. Here we report the structure of human PNP solved to 2.3 Angstrom resolution using synchrotron radiation and cryocrystallographic techniques. This structure allowed a more precise analysis of the active site, generating a more reliable model for substrate binding. The higher resolution data allowed the identification of water molecules in the active site, which suggests binding partners for potential ligands. Furthermore, the present structure may be used in the new structure-based design of PNP inhibitors. (C) 2003 Published by Elsevier B.V.en
dc.description.affiliationUNESP, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationInst Butantan, Ctr Appl Toxicol, BR-05503900 São Paulo, Brazil
dc.description.affiliationUFRGS, Dept Mol Biol & Biotechnol, BR-91501970 Porto Alegre, RS, Brazil
dc.description.affiliationUNESP, Inst Biosci, Dept Biol, Lab Struct Biol & Zoochem CEIS, BR-13506900 Rio Claro, SP, Brazil
dc.description.affiliationPontificia Univ Catolica Rio Grande do Sul, Fac Farm, Inst Pesquisas Biomed, 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, Lab Struct Biol & Zoochem CEIS, BR-13506900 Rio Claro, SP, Brazil
dc.format.extent545-552
dc.identifierhttp://dx.doi.org/10.1016/S0006-291X(03)01431-1
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 308, n. 3, p. 545-552, 2003.
dc.identifier.doi10.1016/S0006-291X(03)01431-1
dc.identifier.issn0006-291X
dc.identifier.lattes9424175688206545
dc.identifier.lattes2901888624506535
dc.identifier.urihttp://hdl.handle.net/11449/19546
dc.identifier.wosWOS:000184945400023
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.titleCrystal structure of human purine nucleoside phosphorylase at 2.3 angstrom resolutionen
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[8]
unesp.author.orcid0000-0002-7363-8211[9]
unesp.author.orcid0000-0003-0903-2407[7]
unesp.author.orcid0000-0003-4971-463X[10]
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