Assessing the Relative Stability of Dimer Interfaces in G Protein-Coupled Receptors
Figure 2
Atomistic structural representations of representative minima of B1AR and B2AR homodimers for the different interfaces.
Panel A shows a view from the cytoplasmic side of the minima Θ1 (dark shades) and Θ2 (lighter shades) for the B1AR (red/pink) and B2AR (blue/light blue) at the TM4/3 interface. The receptors are represented as helices with the loops removed for clarity, and are aligned on the left-most protomer. This panel highlights the small difference between the structures at the same separation but with slightly different angle minima. Panel B shows a view from the cytoplasmic side, of the minima extracted from the FES for the TM1/H8 interface. B1AR is shown in red and B2AR is shown in blue. The intracellular loops are omitted for clarity, and H8 and TM1 are highlighted to indicate the packing of the helices at the interface. Contacting residues are listed in Table S1 and depicted in Fig. S4.