Comparison of the solution structures of angiotensin I & II - Implication for structure-function relationship
Φόρτωση...
Ημερομηνία
Συγγραφείς
Spyroulias, G. A.
Nikolakopoulou, P.
Tzakos, A.
Gerothanassis, I. P.
Magafa, V.
Manessi-Zoupa, E.
Cordopatis, P.
Τίτλος Εφημερίδας
Περιοδικό ISSN
Τίτλος τόμου
Εκδότης
Wiley-Blackwell
Περίληψη
Τύπος
Είδος δημοσίευσης σε συνέδριο
Είδος περιοδικού
peer reviewed
Είδος εκπαιδευτικού υλικού
Όνομα συνεδρίου
Όνομα περιοδικού
European Journal of Biochemistry
Όνομα βιβλίου
Σειρά βιβλίου
Έκδοση βιβλίου
Συμπληρωματικός/δευτερεύων τίτλος
Περιγραφή
Conformational 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.
Περιγραφή
Λέξεις-κλειδιά
angiotensin, nmr, renin-angiotensin system, solid phase peptide synthesis, solution structure, nuclear-magnetic-resonance, receptor-bound conformation, n-terminal domain, at(1) receptor, cyclic analogs, side-chains, active conformation, nmr-spectroscopy, antagonists, proteins
Θεματική κατηγορία
Παραπομπή
Σύνδεσμος
<Go to ISI>://000182717400007
http://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
http://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
Γλώσσα
en
Εκδίδον τμήμα/τομέας
Όνομα επιβλέποντος
Εξεταστική επιτροπή
Γενική Περιγραφή / Σχόλια
Ίδρυμα και Σχολή/Τμήμα του υποβάλλοντος
Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας