Solution structure of an SRYD-containing sequence (250-257) of the fibronectin-like Leishmania gp63 protein by restrained molecular dynamics

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dc.contributor.authorOrlewski, P.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorSakarellos, C.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.issn0929-5666-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9203
dc.rightsDefault Licence-
dc.subjectleishmania gp63en
dc.subject2d nmren
dc.subjectmolecular dynamicsen
dc.subjectdmso solvent boxen
dc.subjectarginine ionic bridgeen
dc.subjectbeta i-turnen
dc.subjectdimethyl-sulfoxideen
dc.subjectrecognition siteen
dc.subjectcell-adhesionen
dc.subjectrgden
dc.subjectpeptidesen
dc.subjectgrgdspen
dc.titleSolution structure of an SRYD-containing sequence (250-257) of the fibronectin-like Leishmania gp63 protein by restrained molecular dynamicsen
heal.abstractThe IASRYDQL synthetic octapeptide (250-257) of the Leishmania major surface glycoprotein gp63 efficiently inhibits parasite attachment to the macrophage receptors in in vitro experiments, and the SRYD-containing tetrapeptide mimics antigenically and functionally the RGDS sequence of fibronectin. The conformational properties of the octapeptide were investigated in dimethylsulfoxide (DMSO) with the combined use of NMR data (vicinal coupling constants, nuclear Overhauser effects (NOEs) and temperature coefficient values), molecular modeling by energy minimization and molecular dynamics. The structure is characterized by the high occurrence, exceeding 95%, of the Arg-Asp side-chain-side-chain ionic interaction, which plays a key role in the backbone folding through a distorted type-I beta-turn involving the Gln(256)-NH to Arg(253)-CO hydrogen bond.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondary<Go to ISI>://A1996WA48200007-
heal.identifier.secondaryhttp://www.springerlink.com/content/h5x231333042l588/fulltext.pdf-
heal.journalNameLetters in Peptide Scienceen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate1996-
heal.publisherKluwer Academic Publishersen
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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