Extended Data Fig. 8: Structural comparison of class A and class B GPCRs in complex with trimeric Gαβγ complexes.
From: PtdIns(4,5)P2 stabilizes active states of GPCRs and enhances selectivity of G-protein coupling
The PtdIns(4,5)P2 contacts of the Gαs subunit observed in molecular dynamics simulations (green spheres) are highlighted on the structures of trimeric G-protein interactions with β2AR (PDB: 3SN6), the glucagon-like peptide-1 receptor (GLP-1) (PDB: 5VAI) and the calcitonin receptor (CTR) (PDB: 5UZ7). Basic residues on the interface adjacent to the cytoplasmic end of TM4 are highlighted as purple spheres. Lower panels show an expanded view, highlighting the conserved pattern of PtdIns(4,5)P2 bridging in class A GPCRs (β2AR and A2AR (Fig. 3e)), both of which have basic residues on TM4 (Lys140 and Arg107/111) that are not present in the class B GPCRs GLP-1R and CTR.
