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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/123456789/9204
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dc.contributor.authorPetit, M. C.en
dc.contributor.authorOrlewski, P.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorTzinia, A.en
dc.contributor.authorKonidou, G.en
dc.contributor.authorSoteriadou, K. P.en
dc.contributor.authorMarraud, M.en
dc.contributor.authorCung, M. T.en
dc.date.accessioned2015-11-24T16:47:33Z-
dc.date.available2015-11-24T16:47:33Z-
dc.identifier.issn0014-2956-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9204-
dc.rightsDefault Licence-
dc.subjectantigen-antibody interactionen
dc.subjectleishmania gp63en
dc.subjectmolecular dynamicsen
dc.subjectsryd motifen
dc.subjecttransferred noeen
dc.subjectmajor surface glycoproteinen
dc.subjectmagnetic-resonance spectroscopyen
dc.subjectmonoclonal-antibodyen
dc.subjectcell-adhesionen
dc.subjectcutaneous leishmaniasisen
dc.subjecteffective immunizationen
dc.subjectprotective immunityen
dc.subjectfibrinogen receptoren
dc.subjectsecondary structureen
dc.subjectzinc-bindingen
dc.titleSolution structures of the fibronectin-like Leishmania gp63 SRYD-containing sequence in the free and antibody-bound states - Transferred NOE and molecular dynamics studiesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://000073002500023-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1046/j.1432-1327.1998.2530184.x/asset/j.1432-1327.1998.2530184.x.pdf?v=1&t=h0e0p1ra&s=7e6b1005887e4f49d9bb126bbc71d16710696f90-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate1998-
heal.abstractThe anti-SRYD monoclonal antibody (mAbSRYD) raised against the IASRYDQL synthetic octapeptide, the 250-257 sequence of the Leishmania major surface glycoprotein gp63 recognizes both SRYD-containing peptides and the whole cognate major surface protein on intact parasites. Two SRYD-containing peptides. which antigenically and functionally mimic the RGDS sequence of fibronectin and efficiently inhibit parasite attachment to the macrophage receptors. were studied by two-dimensional transferred nuclear Overhauser effect experiments in the presence of mAbSRYD. The antibody-bound IASRYDQL octapeptide solution conformation was determined on the basis of 55 interproton-distance restraints, derived from NMR measurements. Eighteen structures which were first generated using an approach combining distance geometry and molecular dynamics, converge by energy minimization toward a folded structure with an average rmsd from the experimental data of less than 0.05 nm for the overall backbone and 0.025 nm for the SRYD motif. A distorted y-turn was found, stabilized by the backbone-backbone D255-NH to R253-CO hydrogen bond, while the R253 and D255 side chains are pointing in opposite directions. This latter antibody-bound structure is compared with that of the free octapeptide in dimethylsulfoxide solution, and with thr crystal structure of the RYD fragment in OPG2 Fab, an antireceptor antibody that mimics the RGD cell adhesion site. On this basis, a mechanism for IASRYDQL-receptor interaction is discussed.en
heal.publisherSpringer-Verlagen
heal.journalNameEuropean Journal of Biochemistryen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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