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. 2020 Oct 15;11:5205. doi: 10.1038/s41467-020-18945-0

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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. 2 — a Detailed interaction between GHRH and the TMD pocket of GHRHR with hydrogen bonds shown as dotted lines. b, c Pairwise comparison of GHRH bound to GHRHR with GLP-1 and LA-PTH in complex with their corresponding receptors, showing the relative positions of peptide ligands. Lime green, GHRHR; blue, GHRH; red, PTH1R and LA-PTH; purple, GLP-1R and GLP-1. d–f The effects of mutation in the ligand-binding pocket on cAMP accumulation. cAMP levels were measured in wild-type (WT) receptor and alanine mutants in ECL1, 2, and 3 (d), TM1, 2, and 3 (e), and TM5, 6, and 7 (f). cAMP signals were normalized to the maximum response of WT and concentration–response curves were analyzed using a three-parameter logistic equation. Data shown are means ± S.E.M. of at least three independent experiments (n = 3–5), conducted in triplicate. Source data are provided as a Source data file.