Rearrangement of the transmembrane domain interfaces associated with the activation of a GPCR hetero-oligomer.
Allosteric Regulation
/ drug effects
Allosteric Site
/ drug effects
Cross-Linking Reagents
/ chemistry
GABA-B Receptor Agonists
/ pharmacology
HEK293 Cells
Humans
Models, Molecular
Protein Binding
/ drug effects
Protein Domains
/ drug effects
Protein Multimerization
/ drug effects
Receptors, GABA-B
/ metabolism
gamma-Aminobutyric Acid
/ metabolism
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
24 06 2019
24 06 2019
Historique:
received:
03
07
2018
accepted:
04
06
2019
entrez:
26
6
2019
pubmed:
27
6
2019
medline:
6
7
2019
Statut:
epublish
Résumé
G protein-coupled receptors (GPCRs) can integrate extracellular signals via allosteric interactions within dimers and higher-order oligomers. However, the structural bases of these interactions remain unclear. Here, we use the GABA
Identifiants
pubmed: 31235691
doi: 10.1038/s41467-019-10834-5
pii: 10.1038/s41467-019-10834-5
pmc: PMC6591306
doi:
Substances chimiques
Cross-Linking Reagents
0
GABA-B Receptor Agonists
0
Receptors, GABA-B
0
gamma-Aminobutyric Acid
56-12-2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2765Subventions
Organisme : Agence Nationale de la Recherche (French National Research Agency)
ID : ANR-09-PIRI-0011
Pays : International
Organisme : Fondation pour la Recherche Médicale (Foundation for Medical Research in France)
ID : DEQ20130326522
Pays : International
Organisme : Fondation pour la Recherche Médicale (Foundation for Medical Research in France)
ID : DEQ20170336747
Pays : International
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