{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yang F"],"funding":["Innovative Program of Development Foundation of Hefei Center for Physical Science and Technology","National Natural Science Foundation of China","National Key Research and Development Project of China"],"pagination":["nwaa284"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11261663"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(9)"],"pubmed_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 β<sub>2</sub>AR-Gα<sub>s</sub>[Formula: see text]γ bound with partial agonist salbutamol or bound with full agonist isoprenaline using"],"journal":["National science review"],"pubmed_title":["Different conformational responses of the β<sub>2</sub>-adrenergic receptor-Gs complex upon binding of the partial agonist salbutamol or the full agonist isoprenaline."],"pmcid":["PMC11261663"],"funding_grant_id":["2018CXFX004","2017YFA0505400","31971152","2016YFA0400903","21825703"],"pubmed_authors":["Ling S","Hu LA","Zhang Y","Fang W","Shi P","Tian C","Liu S","Sun W","Zhang L","Zhou Y","Yang F","Lv P"],"additional_accession":[]},"is_claimable":false,"name":"Different conformational responses of the β<sub>2</sub>-adrenergic receptor-Gs complex upon binding of the partial agonist salbutamol or the full agonist isoprenaline.","description":"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 β<sub>2</sub>AR-Gα<sub>s</sub>[Formula: see text]γ bound with partial agonist salbutamol or bound with full agonist isoprenaline using","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Sep","modification":"2026-06-03T00:21:31.284Z","creation":"2025-06-01T01:16:19.909Z"},"accession":"S-EPMC11261663","cross_references":{"pubmed":["39040950"],"doi":["10.1093/nsr/nwaa284"]}}