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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/7827
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dc.contributor.authorLaimou, D.en
dc.contributor.authorLazoura, E.en
dc.contributor.authorTroganis, A. N.en
dc.contributor.authorMatsoukas, M. T.en
dc.contributor.authorDeraos, S. N.en
dc.contributor.authorKatsara, M.en
dc.contributor.authorMatsoukas, J.en
dc.contributor.authorApostolopoulos, V.en
dc.contributor.authorTselios, T. V.en
dc.date.accessioned2015-11-24T16:34:38Z-
dc.date.available2015-11-24T16:34:38Z-
dc.identifier.issn0920-654X-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/7827-
dc.rightsDefault Licence-
dc.subjectexperimental autoimmune encephalomyelitisen
dc.subjectmultiple sclerosisen
dc.subjectcentral nervous systemen
dc.subjectmyelin basic proteinen
dc.subjectmajor histocompatibility complex class iien
dc.subjectt-cell receptoren
dc.subjectexperimental allergic encephalomyelitisen
dc.subjectexperimental autoimmune encephalomyelitisen
dc.titleConformational studies of immunodominant myelin basic protein 1-11 analogues using NMR and molecular modelingen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDOI 10.1007/s10822-011-9481-6-
heal.identifier.secondary<Go to ISI>://000298191200003-
heal.identifier.secondaryhttp://www.springerlink.com/content/pu573472702h2555/fulltext.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιώνel
heal.publicationDate2011-
heal.abstractTwo dimensional nuclear magnetic resonance studies complimented by molecular dynamics simulations were conducted to investigate the conformation of the immunodominant epitope of acetylated myelin basic protein residues 1-11 (Ac-MBP(1-11)) and its altered peptide ligands, mutated at position 4 to an alanine (Ac-MBP(1-11)[4A]) or a tyrosine residue (Ac-MBP(1-11)[4Y]). Conformational analysis of the three analogues indicated that they adopt an extended conformation in DMSO solution as no long distance NOE connectivities were observed and seem to have a similar conformation when bound to the active site of the major histocompatibility complex (MHC II). The interaction of each peptide with MHC class II I-A(u) was further investigated in order to explore the molecular mechanism of experimental autoimmune encephalomyelitis induction/inhibition in mice. The present findings indicate that the Gln(3) residue, which serves as a T-cell receptor (TCR) contact site in the TCR/peptide/I-A(u) complex, has a different orientation in the mutated analogues especially in the Ac-MBP(1-11)[4A] peptide. In particular the side chain of Gln(3) is not solvent exposed as for the native Ac-MBP(1-11) and it is not available for interaction with the TCR.en
heal.journalNameJournal of Computer-Aided Molecular Designen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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