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dc.creatorDíaz Quintana, Antonio Jesúses
dc.creatorGarcía Mauriño, Sofía M.es
dc.creatorDíaz Moreno, Irenees
dc.date.accessioned2018-01-18T12:34:21Z
dc.date.available2018-01-18T12:34:21Z
dc.date.issued2015
dc.identifier.citationDíaz Quintana, A., García Mauriño, S.M. y Díaz Moreno, I. (2015). Dimerization model of the C-terminal RNA Recognition Motif of HuR. FEBS Letters, 589 (10), 1059-1066.
dc.identifier.issn0014-5793es
dc.identifier.urihttps://hdl.handle.net/11441/69174
dc.description.abstractHuman antigen R (HuR) is a ubiquitous 32kDa protein comprising three RNA Recognition Motifs (RRMs), whose main function is to bind Adenylate and uridylate Rich Elements (AREs) in 3′ UnTranslated Regions (UTRs) of mRNAs. In addition to binding RNA molecules, the third domain (RRM3) is involved in HuR oligomerization and apoptotic signaling. The RRM3 monomer is able to dimerize, with its self-binding affinity being dependent on ionic strength. Here we provide a deeper structural insight into the nature of the encounter complexes leading to the formation of RRM3 dimers by using Brownian Dynamics and Molecular Dynamics. Our computational data show that the initial unspecific encounter follows a downhill pathway until reaching an optimum conformation stabilized by hydrophobic interactions.es
dc.description.sponsorshipJunta de Andalucía P07-CVI-02896, P11-CVI-07216 and 290 BIO198es
dc.formatapplication/pdfes
dc.language.isoenges
dc.publisherwileyes
dc.relation.ispartofFEBS Letters, 589 (10), 1059-1066.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectDimerizationes
dc.subjectHuman antigen R (HuR)es
dc.subjectRNA Binding Proteines
dc.subjectRNA Recognition Motif (RRM)es
dc.subjectBrownian Dynamics (BD)es
dc.subjectMolecular Dynamics (MD)es
dc.titleDimerization model of the C-terminal RNA Recognition Motif of HuRes
dc.typeinfo:eu-repo/semantics/articlees
dc.type.versioninfo:eu-repo/semantics/submittedVersiones
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Moleculares
dc.relation.projectIDP07-CVI-02896es
dc.relation.projectIDP11-CVI-07216es
dc.relation.projectID290 BIO198es
dc.relation.publisherversionhttp://dx.doi.org/10.1016/j.febslet.2015.03.013es
dc.identifier.doi10.1016/j.febslet.2015.03.013es
idus.format.extent7 p.es
dc.journaltitleFEBS Letterses
dc.publication.volumen589es
dc.publication.issue10es
dc.publication.initialPage1059es
dc.publication.endPage1066es
dc.contributor.funderJunta de Andalucía

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