Fig. 5: Side-by-Side structure Comparison of CRF2R-G11 with M1R-G11.
a Superposition of CRF2R-G11 and M1R-G11 (PDB: 6OIJ) complexes. The UCN1-CRF2R-G11 structure is colored cornflower blue (CRF2R), hot pink (G11) and aquamarine (Gα-β1); the M1R-G11 structure is colored green yellow (M1R), light coral (G11) and violet (Gα-β1). b Interaction comparison between ICL2 and G11 in CRF2R-G11 and M1R-G11 structures. Most ICL2 side chains of the receptor, the side chains of N198, I199, and K345 of Gα11 were truncated in the structure. The rotamers of those residues shown in this figure were based on the Rosetta-refined model. c Comparison of TM6, TM7 and H8-Gβ1 conformation in CRF2R-G11 and M1R-G11 complex. d Interactions comparison between CRF2R H8-Gβ1 and M1R H8-Gβ1. The side chains of K372, and D379 of the receptor, and R42 and D312 of Gβ1were truncated in the structure, whose rotamers shown in this panel was from the Rosetta-refined model. e Comparison of positively charged residues in H8 of CRF2R, at the C-terminus of M1R and electrostatic surface potential of G protein. f Comparison of the Gα11-α5-TMD interactions in the CRF2R-G11 and M1R-G11 structures. Hydrogen bonds are shown as purple dashed lines. Most side chains of the receptor, and those of K345, D346 and E355 of Gα11 were truncated in the structure. The rotamers of those residues shown in this figure were based on the Rosetta-refined model.
