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http://purl.uniprot.org/citations/32818430http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32818430http://www.w3.org/2000/01/rdf-schema#comment"Cardiac disease remains the leading cause of morbidity and mortality worldwide. The β1-adrenergic receptor (β1-AR) is a major regulator of cardiac functions and is downregulated in the majority of heart failure cases. A key physiological process is the activation of heterotrimeric G-protein Gs by β1-ARs, leading to increased heart rate and contractility. Here, we use cryo-electron microscopy and functional studies to investigate the molecular mechanism by which β1-AR activates Gs. We find that the tilting of α5-helix breaks a hydrogen bond between the sidechain of His373 in the C-terminal α5-helix and the backbone carbonyl of Arg38 in the N-terminal αN-helix of Gαs. Together with the disruption of another interacting network involving Gln59 in the α1-helix, Ala352 in the β6-α5 loop, and Thr355 in the α5-helix, these conformational changes might lead to the deformation of the GDP-binding pocket. Our data provide molecular insights into the activation of G-proteins by G-protein-coupled receptors."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2020.08.001"xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Huang J."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Liu W."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Su M."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Zhu L."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Walz T."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Williams D."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Huang X.Y."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Lee M.Y."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Hite R.K."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Paknejad N."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Ernst O.P."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Eng E.T."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Dey R."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Jordan K.D."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/author"Meyerson J.R."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/name"Mol Cell"xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/pages"59-71.e4"xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/title"Structural Basis of the Activation of Heterotrimeric Gs-Protein by Isoproterenol-Bound betapisub>1pi/sub>-Adrenergic Receptor."xsd:string
http://purl.uniprot.org/citations/32818430http://purl.uniprot.org/core/volume"80"xsd:string
http://purl.uniprot.org/citations/32818430http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/32818430