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Titolo:
Determination of structural elements related to the biological activities of a potent decapeptide agonist of human C5a anaphylatoxin
Autore:
Vogen, SM; Prakash, O; Kirnarsky, L; Sanderson, SD; Sherman, SA;
Indirizzi:
Univ Nebraska, Ctr Med, Eppley Inst Res Canc & Allied Dis, Omaha, NE 68198USA Univ Nebraska Omaha NE USA 68198 es Canc & Allied Dis, Omaha, NE 68198USA Kansas State Univ, Dept Biochem, Manhattan, KS 66506 USA Kansas State Univ Manhattan KS USA 66506 Biochem, Manhattan, KS 66506 USA
Titolo Testata:
JOURNAL OF PEPTIDE RESEARCH
fascicolo: 1, volume: 54, anno: 1999,
pagine: 74 - 84
SICI:
1397-002X(199907)54:1<74:DOSERT>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
EFFECTOR REGION; CONFORMATION; RECEPTOR; EXPRESSION; PROTEINS; IDENTIFICATION; STIMULATION; PEPTIDES; CELLS; CD88;
Keywords:
agonist; beta-turn; gamma-turn; human C5a; nuclear magnetic resonance;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Sherman, SA Univ Nebraska, Ctr Med, Eppley Inst Res Canc & Allied Dis, 986805 NebraskaMed Ctr, Omaha, NE 68198 USA Univ Nebraska 986805 Nebraska Med Ctr Omaha NE USA 68198 8 USA
Citazione:
S.M. Vogen et al., "Determination of structural elements related to the biological activities of a potent decapeptide agonist of human C5a anaphylatoxin", J PEPT RES, 54(1), 1999, pp. 74-84

Abstract

The structural features related to the biologic activities of a potent, response-selective decapeptide agonist of human C5a, YSFKPMPLaR (C5a(65-74), Y65, F67, P69, P71, D-Ala73), were identified by NMR analysis in H2O, DMSO and TFE. This investigation showed that the KPM residues in H2O and the SFKPM residues in DMSO exhibited an extended backbone conformation, whereas a twisted conformation was found in this region in TFE. In H2O, the C-terminal region (PLaR) adopted a distorted type II beta-turn or a type II/V beta-turn. In the type II/V beta-turn, Leu72 exhibited a conformation typical of a type II beta-turn, whereas D-Ala73 exhibited a conformation characteristic of a type V beta-turn. Furthermore, a gamma-turn involving residues LaR overlapped with the type II/V beta-turn. In DMSO, the C-terminal region had the analogous turn-like motif (type II/V beta-turn overlapping with gamma-turn) found in H2O. In TFE, no beta-turn motifs were formed by the PLaR residues. These turn-like motifs in the C-terminal region of the peptide in both H2O and DMSO were in agreement with the biologically important conformations predicted earlier by a structure-function analysis of a related panel of decapeptide analogs. The motifs determined by the NMR analysis of YSFKPMPLaR in H2O and DMSO may represent structural elements important for C5a agonist activity and thus can be used to design the next generation of C5a agonist, partial agonist and antagonist analogs.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 18:33:11