Comparison of the solution structures of angiotensin I & II - Implication for structure-function relationship

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dc.contributor.authorSpyroulias, G. A.en
dc.contributor.authorNikolakopoulou, P.en
dc.contributor.authorTzakos, A.en
dc.contributor.authorGerothanassis, I. P.en
dc.contributor.authorMagafa, V.en
dc.contributor.authorManessi-Zoupa, E.en
dc.contributor.authorCordopatis, P.en
dc.date.accessioned2015-11-24T16:54:09Z
dc.date.available2015-11-24T16:54:09Z
dc.identifier.issn0014-2956-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10122
dc.rightsDefault Licence-
dc.subjectangiotensinen
dc.subjectnmren
dc.subjectrenin-angiotensin systemen
dc.subjectsolid phase peptide synthesisen
dc.subjectsolution structureen
dc.subjectnuclear-magnetic-resonanceen
dc.subjectreceptor-bound conformationen
dc.subjectn-terminal domainen
dc.subjectat(1) receptoren
dc.subjectcyclic analogsen
dc.subjectside-chainsen
dc.subjectactive conformationen
dc.subjectnmr-spectroscopyen
dc.subjectantagonistsen
dc.subjectproteinsen
dc.titleComparison of the solution structures of angiotensin I & II - Implication for structure-function relationshipen
heal.abstractConformational analysis of angiotensin I (AI) and II (AII) peptides has been performed through 2D (1) H-NMR spectroscopy in dimethylsulfoxide and 2,2,2-trifluoroethanol/H-2 O. The solution structural models of AI and AII have been determined in dimethylsulfoxide using NOE distance and (3) J (HNHalpha) coupling constants. Finally, the AI family of models resulting from restrained energy minimization (REM) refinement, exhibits pairwise rmsd values for the family ensemble 0.26 +/- 0.13 Angstrom, 1.05 +/- 0.23 Angstrom, for backbone and heavy atoms, respectively, and the distance penalty function is calculated at 0.075 +/- 0.006 Angstrom(2) . Comparable results have been afforded for AII ensemble (rmsd values 0.30 +/- 0.22 Angstrom, 1.38 +/- 0.48 Angstrom for backbone and heavy atoms, respectively; distance penalty function is 0.029 +/- 0.003 Angstrom(2) ). The two peptides demonstrate similar N-terminal and different C-terminal conformation as a consequence of the presence/absence of the His9-Leu10 dipeptide, which plays an important role in the different biological function of the two peptides. Other conformational variations focused on the side-chain orientation of aromatic residues, which constitute a biologically relevant hydrophobic core and whose inter-residue contacts are strong in dimethylsulfoxide and are retained even in mixed organic-aqueous media. Detailed analysis of the peptide structural features attempts to elucidate the conformational role of the C-terminal dipeptide to the different binding affinity of AI and AII towards the AT(1) receptor and sets the basis for understanding the factors that might govern free- or bound-depended AII structural differentiation.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primaryDOI 10.1046/j.1432-1033.2003.03573.x-
heal.identifier.secondary<Go to ISI>://000182717400007-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1046/j.1432-1033.2003.03573.x/asset/j.1432-1033.2003.03573.x.pdf?v=1&t=hmn3jvwg&s=db9fa19cf82eab607f2f150c5db001bae50d8b23-
heal.journalNameEuropean Journal of Biochemistryen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2003-
heal.publisherWiley-Blackwellen
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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