Mutations in the NPxxY motif stabilize pharmacologically distinct conformational states of the α
Journal
Science signaling
ISSN: 1937-9145
Titre abrégé: Sci Signal
Pays: United States
ID NLM: 101465400
Informations de publication
Date de publication:
12 03 2019
12 03 2019
Historique:
entrez:
14
3
2019
pubmed:
14
3
2019
medline:
15
5
2020
Statut:
epublish
Résumé
G protein-coupled receptors (GPCRs) convert extracellular stimuli to intracellular responses that regulate numerous physiological processes. Crystallographic and biophysical advances in GPCR structural analysis have aided investigations of structure-function relationships that clarify our understanding of these dynamic receptors, but the molecular mechanisms associated with activation and signaling for individual GPCRs may be more complex than was previously appreciated. Here, we investigated the proposed water-mediated, hydrogen-bonded activation switch between the conserved NPxxY motif on transmembrane helix 7 (TMH7) and a conserved tyrosine in TMH5, which contributes to α
Identifiants
pubmed: 30862702
pii: 12/572/eaas9485
doi: 10.1126/scisignal.aas9485
pii:
doi:
Substances chimiques
Receptors, Adrenergic, alpha-1
0
Receptors, Adrenergic, beta-2
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.