Extended Data Fig. 4: Interface between ICL2 and Gs, for the PCA states A (β2AR-GsGDP intermediate), B, and C (connecting states).
From: Mechanistic insights into G-protein coupling with an agonist-bound G-protein-coupled receptor
A) Residue-residue contact frequencies (interaction cutoff 4 Å) shown as circular flareplots. Residues are represented as dots in a circle and residue-residue contacts as black lines connecting them. The opacity of the line indicates the contact frequency. Moreover, each residue’s secondary structure is displayed with a letter (Helix, Beta-sheet, Coil) next to each dot. Finally, the sum of interactions (interface strength) for each residue is indicated in the outer gray ring, making it easier to locate where the interactions are concentrated, for example in the central region of α5 in state A, the β2AR-GsGDP intermediate. B) Representative structures of states A, B, and C with the interface strength (sum of contact-frequencies per residue) overlaid as a heatmap. ICL2 engages the most with the middle part of α5 and β6 in state A (the β2AR-GsGDP intermediate, on the left). C) Detailed view of the residue-residue interactions at the ICL2 α5/β6 interface in state A (the β2AR-GsGDP intermediate).
