Compared structures of the free nicotinic acetylcholine receptor main immunogenic region (MIR) decapeptide and the antibody-bound [A(76)]MIR analogue: A molecular dynamics simulation from two-dimensional NMR data

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dc.contributor.authorOrlewski, P.en
dc.contributor.authorMarraud, M.en
dc.contributor.authorCung, M. T.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorVatzaki, E.en
dc.contributor.authorTzartos, S. J.en
dc.date.accessioned2015-11-24T16:54:07Z
dc.date.available2015-11-24T16:54:07Z
dc.identifier.issn0006-3525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10118
dc.rightsDefault Licence-
dc.subjectacetylcholine receptoren
dc.subjectmyasthenia gravisen
dc.subjectantigen-antibody interactionen
dc.subjectantigenic peptideen
dc.subjecttwo-dimensional nmren
dc.subjectmolecular dynamicsen
dc.subjectdmso solvent boxen
dc.subjectmonoclonal-antibodiesen
dc.subjectdimethyl-sulfoxideen
dc.subjectalpha-67-76 fragmenten
dc.subjectsynthetic peptidesen
dc.subjectmagnetic-resonanceen
dc.subjectcrystal-structureen
dc.subjectalpha-subuniten
dc.subjectantigenen
dc.subjectresiduesen
dc.subjecttorpedoen
dc.titleCompared structures of the free nicotinic acetylcholine receptor main immunogenic region (MIR) decapeptide and the antibody-bound [A(76)]MIR analogue: A molecular dynamics simulation from two-dimensional NMR dataen
heal.abstractMonoclonal antibodies against the main immunogenic region (MIR) of the muscle acetylcholine receptor (AChR) are capable of inducing experimental myasthenia gravis (MG) in animals. The epitope of these antibodies has been localized between residues 67 and 76 of the AChR cu-subunit. The conformation in solution of the Torpedo californica MIR peptide and of its [A(76)] MIR analogue have been analyzed using molecular modeling based on nmr interproton distances and J-derived phi dihedral angles. Molecular dynamics simulations including dimethyl-sulfoxide as explicit solvent have been carried out on the free MIR peptide. Calculation of the structure of the [A(76)]MIR analogue bound to an anti-MIR monoclonal antibody have been performed in the presence of water molecules. A tightly folded structure appears for bothpeptides with a beta-folded N-terminal N-68-P-A-D-71 sequence of type I in the free state and type III in the mAb6-bound state. The C-terminal sequence is folded in two different ways according to the result in the free and bound state of the peptides: two overlapping beta/beta ar beta/alpha turns result in a short helical sequence in the free MIR peptide, whereas the bound analogue is folded by an uncommon hydrogen bond closing an 11-membered, cycle. This structural evolution is essentially the result of the reorientation of the hydrophobic side chains that are probably directly involved in peptide-antibody recognition. (C) 1997 John Wiley & Sons, Inc.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondary<Go to ISI>://A1996WL15200003-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/(SICI)1097-0282(1996)40:5<419::AID-BIP1>3.0.CO;2-Z/asset/1_ftp.pdf?v=1&t=h0e0nrwa&s=5d5fa41a6a594b2dc75dbd1dae416711e9257eca-
heal.journalNameBiopolymersen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate1996-
heal.publisherWileyen
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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