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Superimpositions of the two tirzepatide- and three peptide 20-bound structures to the three receptors bound by the endogenous ligands (GIP, GLP-1 and GCG) showed that the five peptides all adopt a single continuous helix, with the well-overlapped N terminus penetrating to the TMD core stabilized by conserved interactions, while the C terminus anchors the ECD, ECL1 and ECL2 in a receptor- and ligand-specific manner

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