Different conformational responses of the β₂-adrenergic receptor-Gs complex upon binding of the partial agonist salbutamol or the full agonist isoprenaline.

ABSTRACT: G protein-coupled receptors (GPCRs) are responsible for most cytoplasmic signaling in response to extracellular ligands with different efficacy profiles. Various spectroscopic techniques have identified that agonists exhibiting varying efficacies can selectively stabilize a specific conformation of the receptor. However, the structural basis for activation of the GPCR-G protein complex by ligands with different efficacies is incompletely understood. To better understand the structural basis underlying the mechanisms by which ligands with varying efficacies differentially regulate the conformations of receptors and G proteins, we determined the structures of β₂AR-Gα_s[Formula: see text]γ bound with partial agonist salbutamol or bound with full agonist isoprenaline using

SUBMITTER: Yang F 

PROVIDER: S-EPMC11261663 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature