Fig. 8: Overview of observed β1AR conformational dynamics in response to ligands. | Nature Communications

Fig. 8: Overview of observed β1AR conformational dynamics in response to ligands.

From: A high-resolution description of β1-adrenergic receptor functional dynamics and allosteric coupling from backbone NMR

Fig. 8

Top: overview of conformational averages in various ligand-bound forms: (i) the antagonist complex in fast equilibrium biased to an inactive conformation, (ii) the agonist complex in fast equilibrium biased towards the preactive conformation and in a further slow equilibrium (closing of YY-bridge) with the active conformation, (iii) the ternary agonist•effector protein complex in the fully active conformation. Arrows indicate readouts of conformational averages provided by chemical shifts that correlate to ligand efficacy (V5.57) and affinity (V6.59). YY-bridge residues Y5.58 and Y7.53 are shown in yellow. Bottom: free energy landscape corresponding to the various ligand-bound forms.

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