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The major determinant of exendin‐4/glucagon‐like peptide 1 differential affinity at the rat glucagon‐like peptide 1 receptor N‐terminal domain is a hydrogen bond from SER‐32 of exendin‐4

Exendin‐4 (exenatide, Ex4) is a high‐affinity peptide agonist at the glucagon‐like peptide‐1 receptor (GLP‐1R), which has been approved as a treatment for type 2 diabetes. Part of the drug/hormone binding site was described in the crystal structures of both GLP‐1 and Ex4 bound to the isolated N‐terminal domain (NTD) of GLP‐1R. However, these structures do not account for the large difference in affinity between GLP‐1 and Ex4 at this isolated domain, or for the published role of the C‐terminal extension of Ex4. Our aim was to clarify the pharmacology of GLP‐1R in the context of these new structural data.