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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/9198
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dc.contributor.authorPhan-Chan-Du, A.en
dc.contributor.authorHemmerlin, C.en
dc.contributor.authorKrikorian, D.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorMarinou, M.en
dc.contributor.authorThureau, A.en
dc.contributor.authorCung, M. T.en
dc.contributor.authorTzartos, S. J.en
dc.date.accessioned2015-11-24T16:47:31Z-
dc.date.available2015-11-24T16:47:31Z-
dc.identifier.issn0006-2960-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9198-
dc.rightsDefault Licence-
dc.subjectphase peptide-synthesisen
dc.subjectmonoclonal-antibodiesen
dc.subjectgamma-subuniten
dc.subjectmolecular-dynamicsen
dc.subjectalpha-subuniten
dc.subjectproteinsen
dc.subjectspectroscopyen
dc.subjectnmren
dc.subjectregionen
dc.subjectprobesen
dc.titleSolution conformation of the antibody-bound tyrosine phosphorylation site of the nicotinic acetylcholine receptor beta-subunit in its phosphorylated and nonphosphorylated statesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1021/Bi030034u-
heal.identifier.secondary<Go to ISI>://000183624800011-
heal.identifier.secondaryhttp://pubs.acs.org/doi/pdfplus/10.1021/bi030034u-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2003-
heal.abstractPhosphorylation of the acetylcholine receptor (AChR) seems to be responsible for triggering several effects including its desensitization and aggregation at the postsynaptic membrane and probably initiates a signal transduction pathway at the postsynaptic membrane. To study the structural and functional role of the tyrosine phosphorylation site of the AChR beta-subunit and contribute to the in-depth understanding of the structural basis of the ion channel function, we synthesized four peptides containing the phosphorylated and nonphosphorylated sequences (380-391) of the human and Torpedo AChR beta-subunits and studied their interaction with a monoclonal antibody (mAb 148) that is known to bind to this region and that is capable of blocking ion channel function. All four peptides were efficient inhibitors of mAb 148 binding to AChR, although the nonphosphorylated human peptide was considerably less effective than the three others. We then investigated the conformation acquired by all four peptides in their antibody-bound state, which possibly illustrates the local conformation of the corresponding sites on the intact AChR molecule. The phosphorylated human and Torpedo peptides adopted a distorted 310 helix conformation. The nonphosphorylated Torpedo peptide, which is also an efficient inhibitor, was also folded. In contrast, the nonphosphorylated human peptide (a less efficient inhibitor) presented an extended structure. It is concluded that the phosphorylation of the AChR at its beta-subunit Tyr site leads to a significant change in its conformation, which may affect several functions of the AChR.en
heal.publisherAmerican Chemical Societyen
heal.journalNameBiochemistryen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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