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. Author manuscript; available in PMC: 2021 Oct 1.
Published in final edited form as: Mol Cell. 2020 Aug 19;80(1):59–71.e4. doi: 10.1016/j.molcel.2020.08.001

Figure 6. Conformational changes of the GDP/GTP-binding pocket after β1-AR interaction.

Figure 6.

(A) Comparison of the β1 strand, α1-helix and the β1-α1 loop of the Ras-like domains from β1-AR–Gs (in green) and from Gαs:GTPγS (in gray) when the Ras-like domains are superimposed. (B) Comparison of Switch II region from β1-AR–Gs and from Gαs:GTPγS. (C) Comparison of Switch III region from β1-AR–Gs and from Gαs:GTPγS. (D) Comparison of the regions from αG to α5-helix from β1-AR–Gs and from Gαs:GTPγS. (E) Comparison of all GTP-interacting residues of the Ras-like domains from β1-AR–Gs and from Gαs:GTPγS. (F) Disruptions of intramolecular interactions of Gαs during Gs activation by β1-AR. An ionic lock between the sidechain of His373 in the α5-helix and the backbone carbonyl of Arg38 in the αN-helix is broken. An interacting network involving the sidechain of Gln59 in the α1-helix, the backbone carbonyl of Ala352 in the β6-α5 loop, and the sidechain of Thr355 in the α5-helix is disrupted.