Extended Data Fig. 8. Conformational changes of the GDP-binding pocket of Gα_s after β₁-AR interaction.

(a) Comparison of the β₁ strand, α₁-helix and the β₁-α₁ loop of the Ras-like domains from β₁-AR-Gs (in violet) and from Gα_sGβ₁Gγ₂ (PDB: 6EG8; in teal) when the Ras-like domains are superimposed. (b) Comparison of Switch II region from β₁-AR-Gs and from Gα_sGβ₁Gγ₂. (c) Comparison of Switch III region from β₁-AR-Gs and from Gα_sGβ₁Gγ₂(d) Comparison of the regions from αG to α5-helix from β-₁AR-Gs and from Gα_sGβ₁Gγ₂. (e) Comparison of all GDP-interacting residues of the Ras-like domains from β₁-AR-Gs and from Gα_sGβ₁Gγ₂.(f) Disruptions of intra-molecular interactions of Gα_s during Gs activation by β₁-AR. An interaction between the sidechain of His373 in the α5-helix and the backbone of Arg38 in the αN-helix is broken. An interacting network involving the sidechain of Gln59 in the αl-helix, the backbone carbonyl of Ala352 in the β6-α5 loop, and the sidechain of Thr355 in the α5-helix is disrupted.