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dc.creatorDíaz Moreno, Irenees
dc.creatorHollingworth, Davides
dc.creatorKelly, Geoffes
dc.creatorMartin, Stephenes
dc.creatorGarcía Mayoral, María Flores
dc.date.accessioned2017-08-31T11:46:46Z
dc.date.available2017-08-31T11:46:46Z
dc.date.issued2010
dc.identifier.citationDíaz Moreno, I., Hollingworth, a., Kelly, G., Martin, S. y García Mayoral, M.F. (2010). Orientation of the central domains of KSRP and its implications for the interaction with the RNA targets. Nucleic Acids Research, 38 (15), 5193-5205.
dc.identifier.issn1362-4962 (Electrónico)es
dc.identifier.issn0305-1048 (impreso)es
dc.identifier.urihttp://hdl.handle.net/11441/64106
dc.description.abstractKSRP is a multi-domain RNA-binding protein that recruits the exosome-containing mRNA degradation complex to mRNAs coding for cellular proliferation and inflammatory response factors. The selectivity of this mRNA degradation mechanism relies on KSRP recognition of AU-rich elements in the mRNA 3′UTR, that is mediated by KSRP’s KH domains. Our structural analysis shows that the inter-domain linker orients the two central KH domains of KSRP—and their RNA-binding surfaces—creating a two-domain unit. We also show that this inter-domain arrangement is important to the interaction with KSRP’s RNA targets.es
dc.formatapplication/pdfes
dc.language.isoenges
dc.publisherOxford University Presses
dc.relation.ispartofNucleic Acids Research, 38 (15), 5193-5205.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.titleOrientation of the central domains of KSRP and its implications for the interaction with the RNA targetses
dc.typeinfo:eu-repo/semantics/articlees
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessrightsinfo:eu-repo/semantics/openAccesses
dc.relation.publisherversionhttp://dx.doi.org/10.1093/nar/gkq216es
dc.identifier.doi10.1093/nar/gkq216es
idus.format.extent12 p.es
dc.journaltitleNucleic Acids Researches
dc.publication.volumen38es
dc.publication.issue15es
dc.publication.initialPage5193es
dc.publication.endPage5205es

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