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Titolo:
COMPARISON OF THE STRUCTURE-ACTIVITY-RELATIONSHIPS OF NOCICEPTIN AND DYNORPHIN-A USING CHIMERIC PEPTIDES
Autore:
LAPALU S; MOISAND C; MAZARGUIL H; CAMBOIS G; MOLLEREAU C; MEUNIER JC;
Indirizzi:
CNRS,INST PHARMACOL & BIOL STRUCT,UNITE NEUROPHARMACOL MOL,205 ROUTE NARBONNE F-31077 TOULOUSE 4 FRANCE CNRS,INST PHARMACOL & BIOL STRUCT,UNITE NEUROPHARMACOL MOL F-31077 TOULOUSE 4 FRANCE
Titolo Testata:
FEBS letters
fascicolo: 3, volume: 417, anno: 1997,
pagine: 333 - 336
SICI:
0014-5793(1997)417:3<333:COTSON>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
KAPPA-OPIOID RECEPTOR; PROTEIN-COUPLED RECEPTOR; MOLECULAR-CLONING; ORPHANIN-FQ; GENE FAMILY; TISSUE DISTRIBUTION; CDNA CLONING; MEMBER; NEUROPEPTIDE; LOCALIZATION;
Keywords:
STRUCTURE-ACTIVITY RELATIONSHIP; DYNORPHIN A; NOCICEPTIN ORPHANIN-FQ; CHIMERIC NEUROPEPTIDE; OPIOID AND OPIOID RECEPTOR-LIKE RECEPTOR;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
22
Recensione:
Indirizzi per estratti:
Citazione:
S. Lapalu et al., "COMPARISON OF THE STRUCTURE-ACTIVITY-RELATIONSHIPS OF NOCICEPTIN AND DYNORPHIN-A USING CHIMERIC PEPTIDES", FEBS letters, 417(3), 1997, pp. 333-336

Abstract

The aim of the present study was to delineate the functional domains of nociceptin (noc), a neuropeptide which is structurally related to dynorphin A (dyn), The binding and biological potencies towards the nociceptin (ORL1) and dynarphin A (kappa-opioid) receptors of twenty dyn/noc and noc/dyn hybrid peptides were compared with those of the parentheptadecapeptides. Replacement of as many as eleven residues in the C-terminus of dynorphin by the corresponding nociceptin sequence has nosignificant effect on binding and biological activity towards the kappa-opioid receptor, In marked contrast, replacement of as few as six residues (RKLANQ) in the C-terminus of nociceptin by the corresponding dynorphin sequence (LKWDNQ) dramatically impairs both affinity and activity towards the ORL1 receptor, This clearly indicates that the two neuropeptides have different functional architectures, despite the dualstructural homology of both ligands and receptors, Moreover, the recombinant peptide approach led us to identify hybrids whose sequences differ only at positions 5 and 6 and displaying opposite or no receptor selectivity, One contains the dynorphin sequence and prefers the kappa-opioid receptor, whereas Leu(5)-Arg(6) sequence the other comprises the nociceptin Thr(5)-Gly(6) and prefers the ORL1 receptor. A third, containing the mixed dynorphin/nociceptin Leu(5)-Gly(6) sequence, does not discriminate between the two types of receptor. (C) 1997 Federationof European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 07:43:53