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. 2022 Jun 29;13:891586. doi: 10.3389/fendo.2022.891586

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Copyright © 2022 Lindquist, Gasbjerg, Mokrosinski, Holst, Hauser and Rosenkilde

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Class B1 ligands and the structural perspective. (A) Sequence alignment of related class B1 ligands and peptide analogs. Sequence alignment of glucose-dependent insulinotropic polypeptide (GIP), tirzepatide (dual GIPR/GLP-1R agonist), glucagon-like peptide-1 (GLP-1), semaglutide (GLP-1 analog), GLP-2, teduglutide (GLP-2 analog), glucagon, and oxyntomodulin. A ‘X’ denotes α-aminoisobutyric acid (Aib). Amino acids displayed by black letters represent sites deviating from those of the endogenous peptide. Conserved positions across all peptides are highlighted in grey. (B) Highlighted ligand-receptor interactions between GIP and the GIPR. 3D visualization of GIP(1-30) (blue) in complex with the GIPR (grey) and the Gα_s protein (grey) (Protein Data Bank: 7DTY) (57). Frames to the right display important hydrophobic interactions and polar interactions (yellow dotted lines) between GIPR (grey) and GIP (blue).