Fig. 2: Structural comparison of GIPR, GLP-1R and GCGR bound by mono-, dual and triple agonists. | Nature Communications

Fig. 2: Structural comparison of GIPR, GLP-1R and GCGR bound by mono-, dual and triple agonists.

From: Structural insights into multiplexed pharmacological actions of tirzepatide and peptide 20 at the GIP, GLP-1 or glucagon receptors

Fig. 2

a Structural comparison of GIP–GIPR–Gs25, tirzepatide–GIPR–Gs and peptide 20–GIPR–Gs. Receptor ECD and G protein are omitted for clarity. b Comparison of residue interactions employed by GIPR to recognize GIP, tirzepatide and peptide 20, described by fingerprint strings encoding different interaction types of the surrounding residues in each peptide. Color codes are listed on the top panel. Residues that show no interaction with ligands are displayed as white circles. c Structural comparison of GLP-1–GLP-1R–Gs27, tirzepatide–GLP-1R–Gs and peptide 20–GLP-1R–Gs. Receptor ECD and G protein are omitted for clarity. d Comparison of residue interactions that GLP-1R employed to recognize GLP-1, tirzepatide and peptide 20, described by fingerprint strings encoding different interaction types of the surrounding residues in each peptide. e Structural comparison of GCG–GCGR–Gs4, peptide 15–GCGR–Gs28 and peptide 20–GCGR–Gs. Receptor ECD and G protein are omitted for clarity. f Comparison of residue interactions that GCGR employed to recognize GCG, peptide 15 and peptide 20, described by fingerprint strings encoding different interaction types of the surrounding residues in each peptide.

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