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Titolo:
DIFFERENT DOMAINS OF THE ORL1 AND KAPPA-OPIOID RECEPTORS ARE INVOLVEDIN RECOGNITION OF NOCICEPTIN AND DYNORPHIN-A
Autore:
LAPALU S; MOISAND C; BUTOUR JL; MOLLEREAU C; MEUNIER JC;
Indirizzi:
CNRS UPR 9062,INST PHARMACOL & BIOL STRUCT F-31077 TOULOUSE 4 FRANCE CNRS UPR 9062,INST PHARMACOL & BIOL STRUCT F-31077 TOULOUSE 4 FRANCE
Titolo Testata:
FEBS letters
fascicolo: 2, volume: 427, anno: 1998,
pagine: 296 - 300
SICI:
0014-5793(1998)427:2<296:DDOTOA>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-COUPLED RECEPTOR; MOLECULAR-CLONING; GENE FAMILY; TISSUE DISTRIBUTION; CDNA CLONING; ORPHANIN-FQ; MEMBER; LOCALIZATION; NEUROPEPTIDE; SELECTIVITY;
Keywords:
NON-OPIOID-OPIOID HYBRID RECEPTOR; GAIN-OF-FUNCTION PROTEIN ENGINEERING; OPIOID PEPTIDE; STRUCTURE-FUNCTION RELATIONSHIP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
S. Lapalu et al., "DIFFERENT DOMAINS OF THE ORL1 AND KAPPA-OPIOID RECEPTORS ARE INVOLVEDIN RECOGNITION OF NOCICEPTIN AND DYNORPHIN-A", FEBS letters, 427(2), 1998, pp. 296-300

Abstract

In order to gain further insight into the functional architecture of structurally related G protein-coupled receptors, the ORL1 (nociceptin) and opioid receptors, we have constructed chimeras of ORL1 and mu-, delta and kappa-opioid receptors, and compared their binding and functional properties with those of the parent receptors, We find in particular that a ORL1-kappa-opioid (O-K) hybrid construct has retained highaffinity for non-type-selective opiate ligands, and has acquired the ability to bind and respond to enkephalins and mu- and/or delta-opioidreceptor-selective enkephalins analogs, thus behaving like a 'universal' opioid receptor, Most significantly however, whilst the ORL1 and kappa-opioid receptors display high binding preference (K-D 0.1 vs. 100nM) for their respective endogenous ligands, nociceptin and dynorphinA, the O-K chimeric receptor binds both nociceptin and dynorphin A, with high affinity (K-D < 1 nM). Together, these data (i) add weight tothe hypothesis that the extracellular loops of opioid receptors act as a filter for ligand selection, and (ii) demonstrate that different domains of the ORL1 and kappa-opioid receptors are involved in recognition of their endogenous peptide ligands. (C) 1998 Federation of European Biochemical Societies.

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Documento generato il 06/07/20 alle ore 08:18:49