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. Author manuscript; available in PMC: 2019 Jan 11.
Published in final edited form as: Nature. 2018 Jul 11;559(7714):423–427. doi: 10.1038/s41586-018-0325-6

Extended Data Figure 8. Structural comparison of class A and class B GPCRs in complex with trimeric Gαβγ complexes.

Extended Data Figure 8

The PIP2 contacts of the Gαs subunit observed in MD simulation (green spheres) were highlighted on the structures of trimeric G interactions with β2-adrenergic receptor (β2AR) (PDB: 3SN6), the glucagon-like peptide-1 receptor (GLP-1) (PDB: 5VAI), and the calcitonin receptor (CTR) (PDB: 5UZ7). The basic residues on the interface adjacent to the cytoplasmic end of TM4 are also highlighted (purple spheres). Expansion indicates the conserved pattern of PIP2 bridging in class A GPCRs (β2AR and A2AR (Fig. 3e)) both of which have basic residues on TM4 (Lys140 and Arg107/111) which are not observed in class B GPCRs GLP-1R and CTR.