Recognition pliability is coupled to structural heterogeneity: a calmodulin intrinsically disordered binding region complex

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dc.contributor.authorNagulapalli, M.en
dc.contributor.authorParigi, G.en
dc.contributor.authorYuan, J.en
dc.contributor.authorGsponer, J.en
dc.contributor.authorDeraos, G.en
dc.contributor.authorBamm, V. V.en
dc.contributor.authorHarauz, G.en
dc.contributor.authorMatsoukas, J.en
dc.contributor.authorde Planque, M. R.en
dc.contributor.authorGerothanassis, I. P.en
dc.contributor.authorBabu, M. M.en
dc.contributor.authorLuchinat, C.en
dc.contributor.authorTzakos, A. G.en
dc.date.accessioned2015-11-24T16:46:11Z
dc.date.available2015-11-24T16:46:11Z
dc.identifier.issn1878-4186-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9042
dc.rightsDefault Licence-
dc.subjectBinding Sites/geneticsen
dc.subjectCalmodulin/*chemistry/metabolismen
dc.subject*Models, Molecularen
dc.subjectMultiprotein Complexes/*chemistry/metabolismen
dc.subjectMyelin Basic Protein/*chemistry/metabolismen
dc.subjectNuclear Magnetic Resonance, Biomolecularen
dc.subjectProtein Bindingen
dc.subject*Protein Conformationen
dc.titleRecognition pliability is coupled to structural heterogeneity: a calmodulin intrinsically disordered binding region complexen
heal.abstractProtein interactions within regulatory networks should adapt in a spatiotemporal-dependent dynamic environment, in order to process and respond to diverse and versatile cellular signals. However, the principles governing recognition pliability in protein complexes are not well understood. We have investigated a region of the intrinsically disordered protein myelin basic protein (MBP(145-165)) that interacts with calmodulin, but that also promiscuously binds other biomolecules (membranes, modifying enzymes). To characterize this interaction, we implemented an NMR spectroscopic approach that calculates, for each conformation of the complex, the maximum occurrence based on recorded pseudocontact shifts and residual dipolar couplings. We found that the MBP(145-165)-calmodulin interaction is characterized by structural heterogeneity. Quantitative comparative analysis indicated that distinct conformational landscapes of structural heterogeneity are sampled for different calmodulin-target complexes. Such structural heterogeneity in protein complexes could potentially explain the way that transient and promiscuous protein interactions are optimized and tuned in complex regulatory networks.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primary10.1016/j.str.2012.01.021-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/22405011-
heal.identifier.secondaryhttp://ac.els-cdn.com/S0969212612000524/1-s2.0-S0969212612000524-main.pdf?_tid=a69c3db2-4075-11e3-915b-00000aab0f6b&acdnat=1383036160_64f32c7f993f4fe2da48b6c71b1debf3-
heal.journalNameStructureen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2012-
heal.publisherElsevieren
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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