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Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha

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dc.contributor.authorFontes, Marcos
dc.contributor.authorTeh, Trazel
dc.contributor.authorJans, David A
dc.contributor.authorBrinkworth, Ross I
dc.contributor.authorKobe, Bostjan
dc.date.accessioned2015-12-13T22:31:38Z
dc.date.available2015-12-13T22:31:38Z
dc.date.issued2003
dc.date.updated2015-12-11T09:01:52Z
dc.description.abstractImportin-α 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
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/1885/75342
dc.publisherAmerican Society for Biochemistry and Molecular Biology Inc
dc.sourceJournal of Biological Chemistry
dc.subjectKeywords: Conformations; Crystallization; Proteins; Nuclear localization sequences (NLS); Biochemistry; karyopherin alpha; phosphoprotein; phosphoprotein n1n2; retinoblastoma protein; unclassified drug; article; binding affinity; cell nucleus; crystallization; huma
dc.titleStructural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha
dc.typeJournal article
local.bibliographicCitation.issue30
local.bibliographicCitation.lastpage27987
local.bibliographicCitation.startpage27981
local.contributor.affiliationFontes, Marcos, University of Queensland
local.contributor.affiliationTeh, Trazel, St Vincent's Institute of Medical Research
local.contributor.affiliationJans, David A, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationBrinkworth, Ross I, University of Queensland
local.contributor.affiliationKobe, Bostjan, St Vincent's Institute of Medical Research
local.contributor.authoruidJans, David A, u9306667
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor110302 - Clinical Chemistry (diagnostics)
local.identifier.ariespublicationMigratedxPub4580
local.identifier.citationvolume278
local.identifier.doi10.1074/jbc.M303275200
local.identifier.scopusID2-s2.0-0041845285
local.type.statusPublished Version

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