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Tytuł pozycji:

Replacement of Gln280 by His in TM6 of the human ORL1 receptor increases affinity but reduces intrinsic activity of opioids.

Tytuł :
Replacement of Gln280 by His in TM6 of the human ORL1 receptor increases affinity but reduces intrinsic activity of opioids.
Wydawca :
1996-10
Dodane szczegóły :
Mollereau, Catherine
Moisand, C
Butour, J L
Parmentier, Marc
Meunier, J C
Typ dokumentu :
Zasób elektroniczny
Index Terms :
Sciences bio-médicales et agricoles
Adenylate Cyclase -- antagonists & inhibitors
Animals
Binding, Competitive
CHO Cells
Cell Membrane -- chemistry
Cricetinae
Diprenorphine -- pharmacology
Dynorphins -- metabolism
Etorphine -- metabolism
Fentanyl -- analogs & derivatives
Fentanyl -- metabolism
Glutamine
Histamine
Humans
Kinetics
Ligands
Naltrexone -- analogs & derivatives
Naltrexone -- metabolism
Narcotics -- metabolism
Opioid Peptides -- metabolism
Opioid Peptides -- pharmacology
Receptors, Opioid -- agonists
Receptors, Opioid -- antagonists & inhibitors
Receptors, Opioid -- chemistry
Receptors, Opioid -- genetics
Receptors, Opioid -- metabolism
Adenylate cyclase inhibition
Agonist/antagonist binding
Nociceptin/orphanin FQ
Opioid receptor
Site-directed mutagenesis
info:eu-repo/semantics/article
info:ulb-repo/semantics/articlePeerReview
info:ulb-repo/semantics/openurl/article
URL :
http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/58906">http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/58906
http://worldcat.org/search?q=on:EQY+http://difusion-oai.ulb.ac.be/oai/request+DCG_ENTIRE_REPOSITORY+CNTCOLL">http://worldcat.org/search?q=on:EQY+http://difusion-oai.ulb.ac.be/oai/request+DCG_ENTIRE_REPOSITORY+CNTCOLL
Dostępność :
Open access content. Open access content
1 full-text file(s): info:eu-repo/semantics/restrictedAccess
Uwaga :
1 full-text file(s): application/pdf
English
Pozostałe numery :
EQY oai:dipot.ulb.ac.be:2013/58906
764594928
Źródło wspomagające :
UNIV LIBR DE BRUXELLES
From OAIster®, provided by the OCLC Cooperative.
Numer akcesji :
edsoai.ocn764594928
Zasób elektroniczny
The ORL1 (Opioid Receptor-Like) receptor is the G protein-coupled receptor whose amino acid sequence is closest to those of opioid receptors. Residues that are conserved in ORL1 and the three types of opioid receptor, but also a residue, His in the sixth putative transmembrane (TM6) helix, which is present in all opioid receptor types but absent in ORL1, appear to play a key role in receptor recognition and/or activation. Here we have sought to create an opioid binding pocket in the non-opioid ORL1 receptor by replacing residue Gln280 in its TM6 by the corresponding His residue of opioid receptors. The mutation affects neither the affinity of nociceptin - the natural ORL1 agonist - for the receptor, nor the potency of nociceptin to inhibit adenylyl cyclase via ORL1. In contrast, we find that a few opioid ligands, the agonists lofentanil, etorphine and dynorphin A, and especially the antagonists diprenorphine and nor-BNI, bind the mutant Q280H receptor with substantially (5- to > 100-fold) higher apparent affinity than they do the wild-type receptor. Moreover, lofentanil and etorphine no longer act as pure agonists, as they do at the native ORL1 receptor, but are endowed with clear antagonist properties at the mutant receptor. The mutation Q280H, which increases affinity while decreasing intrinsic activity of opioids at ORL1, emphasizes the importance of the His residue for opioid recognition and activation.
Journal Article
Research Support, Non-U.S. Gov't
SCOPUS: ar.j
info:eu-repo/semantics/published

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