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dc.contributor.authorFontes, MRM
dc.contributor.authorTeh, T.
dc.contributor.authorJans, D.
dc.contributor.authorBrinkworth, R. I.
dc.contributor.authorKobe, B.
dc.date.accessioned2014-05-20T13:49:25Z
dc.date.available2014-05-20T13:49:25Z
dc.date.issued2003-07-25
dc.identifierhttp://dx.doi.org/10.1074/jbc.M303275200
dc.identifier.citationJournal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc., v. 278, n. 30, p. 27981-27987, 2003.
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/11449/17620
dc.description.abstractImportin-alpha is the nuclear import receptor that recognizes cargo proteins carrying conventional basic monopartite and bipartite nuclear localization sequences (NLSs) and facilitates their transport into the nucleus. Bipartite NLSs contain two clusters of basic residues, connected by linkers of variable lengths. To determine the structural basis of the recognition of diverse bipartite NLSs by mammalian importin-alpha, we co-crystallized a non-autoinhibited mouse receptor protein with peptides corresponding to the NLSs from human retinoblastoma protein and Xenopus laevis phosphoprotein N1N2, containing diverse sequences and lengths of the linker. We show that the basic clusters interact analogously in both NLSs, but the linker sequences adopt different conformations, whereas both make specific contacts with the receptor. The available data allow us to draw general conclusions about the specificity of NLS binding by importin-alpha and facilitate an improved definition of the consensus sequence of a conventional basic/bipartite NLS (KRX10-12KRRK) that can be used to identify novel nuclear proteins.en
dc.format.extent27981-27987
dc.language.isoeng
dc.publisherAmer Soc Biochemistry Molecular Biology Inc
dc.relation.ispartofJournal of Biological Chemistry
dc.sourceWeb of Science
dc.titleStructural basis for the specificity of bipartite nuclear localization sequence binding by importin-alphaen
dc.typeArtigo
dcterms.licensehttp://www.jbc.org/site/misc/Copyright_Permission.xhtml
dcterms.rightsHolderAmer Soc Biochemistry Molecular Biology Inc
dc.contributor.institutionSt Vincents Inst Med Res
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniv Queensland
dc.contributor.institutionAustralian Natl Univ
dc.contributor.institutionMonash Univ
dc.description.affiliationSt Vincents Inst Med Res, Struct Biol Lab, Fitzroy, Vic 3065, Australia
dc.description.affiliationUniv Estadual Paulista, UNESP, Inst Biociencias, Dept Fis & Biofis, BR-18618000 Botucatu, SP, Brazil
dc.description.affiliationUniv Queensland, Dept Biochem & Mol Biol, Inst Mol Biosci, Australian Res Council Special Res Ctr Funct & Ap, Brisbane, Qld 4072, Australia
dc.description.affiliationUniv Queensland, Cooperat Res Ctr Chron Inflammatory Dis, Brisbane, Qld 4072, Australia
dc.description.affiliationAustralian Natl Univ, John Curtin Sch Med Res, Div Biochem & Mol Biol, Nucl Signalling Lab, Canberra, ACT 2601, Australia
dc.description.affiliationMonash Univ, Dept Biochem & Mol Biol, Clayton, Vic 3168, Australia
dc.description.affiliationUnespUniv Estadual Paulista, UNESP, Inst Biociencias, Dept Fis & Biofis, BR-18618000 Botucatu, SP, Brazil
dc.identifier.doi10.1074/jbc.M303275200
dc.identifier.wosWOS:000184242700082
dc.rights.accessRightsAcesso restrito
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Botucatupt
unesp.author.orcid0000-0001-9413-9166[5]
unesp.author.orcid0000-0002-4634-6221[1]
dc.relation.ispartofjcr4.010
dc.relation.ispartofsjr2,672
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