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. 2020 Nov 25;30(12):1098–1108. doi: 10.1038/s41422-020-00442-0

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — a Structural comparison of GLP-2–GLP-2R–G_s and GLP-1–GLP-1R–G_s^.13 Receptor ECD and G protein are omitted for clarity. b Schematic diagram of interactions between peptide and receptor. Conserved residues in GLP-2 and GLP-1 are highlighted in pink, while those similar are shown in light pink. Length of gray shading box illustrates the interface area between peptide and corresponding segment. c Signaling profiles of the chimeric GLP-2/GLP-1 peptides. Replacement of the N-terminus (residues 1–6), middle region (residues 7–19) and C-terminus (residues 20–33) of GLP-2 by corresponding segment of GLP-1 was named as chimeric GLP-2/GLP-1(1–6), GLP-2/GLP-1(7–19) and GLP-2/GLP-1(20–33), respectively. Dose-response curves of peptide-induced cAMP accumulation for GLP-2R were generated and graphed as means ± SEM from three independent experiments.