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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/24205
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dc.contributor.authorJoseph, C.en
dc.contributor.authorStier, G.en
dc.contributor.authorO'Brien, R.en
dc.contributor.authorPolitou, A. S.en
dc.contributor.authorAtkinson, R. A.en
dc.contributor.authorBianco, A.en
dc.contributor.authorLadbury, J. E.en
dc.contributor.authorMartin, S. R.en
dc.contributor.authorPastore, A.en
dc.date.accessioned2015-11-24T19:39:02Z-
dc.date.available2015-11-24T19:39:02Z-
dc.identifier.issn0006-2960-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/24205-
dc.rightsDefault Licence-
dc.subjectActinin/*chemistry/genetics/metabolismen
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectCalorimetryen
dc.subjectCircular Dichroismen
dc.subjectEF Hand Motifs/geneticsen
dc.subjectEscherichia coli/geneticsen
dc.subjectHumansen
dc.subjectMagnetic Resonance Spectroscopyen
dc.subjectMolecular Sequence Dataen
dc.subjectMuscle Proteins/*chemistry/metabolismen
dc.subjectPeptide Fragments/*chemistry/geneticsen
dc.subjectProtein Binding/geneticsen
dc.subjectProtein Foldingen
dc.subjectProtein Kinases/*chemistry/metabolismen
dc.subjectProtein Structure, Secondaryen
dc.subjectProtein Structure, Tertiary/geneticsen
dc.subjectRabbitsen
dc.subjectRecombinant Fusion Proteins/chemistry/metabolismen
dc.subject*Repetitive Sequences, Amino Acid/geneticsen
dc.subjectStructure-Activity Relationshipen
dc.titleA structural characterization of the interactions between titin Z-repeats and the alpha-actinin C-terminal domainen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/11305911-
heal.identifier.secondaryhttp://pubs.acs.org/doi/pdfplus/10.1021/bi002739r-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2001-
heal.abstractTitin and alpha-actinin, two modular muscle proteins, are with actin the major components of the Z-band in vertebrate striated muscles where they serve to organize the antiparallel actin filament arrays in adjacent sarcomeres and to transmit tension between sarcomeres during activation. Interactions between titin and alpha-actinin have been mainly localized in a 45-amino acid multiple motif (Z-repeat) in the N-terminal region of titin and the C-terminal region of alpha-actinin. In this study, we provide the first quantitative characterization of alpha-actinin-Z-repeat recognition and dissect the interaction to its minimal units. Different complementary techniques, such as circular dichroism, calorimetry, and nuclear magnetic spectroscopy, were used. Two overlapping alpha-actinin constructs (Act-EF34 and Act-EF1234) containing two and four EF-hand motifs, respectively, were produced, and their folding properties were examined. Complex formation of Act-EF34 and Act-EF1234 with single- and double-Z-repeat constructs was studied. Act-EF34 was shown quantitatively to be necessary and sufficient for binding to Z-repeats, excluding the presence of additional high-affinity binding sites in the remaining part of the domain. The binding affinities of the different Z-repeats for Act-EF34 range from micromolar to millimolar values. The strongest of these interactions are comparable to those observed in troponin C-troponin I complexes. The binding affinities for Act-EF34 are maximal for Zr1 and Zr7, the two highly homologous sequences present in all muscle isoforms. No cooperative or additional contributions to the interaction were observed for Z-repeat double constructs. These findings have direct relevance for evaluating current models of Z-disk assembly.en
heal.journalNameBiochemistryen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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