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. 2022 Oct 21;13:6276. doi: 10.1038/s41467-022-34009-x

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© The Author(s) 2022

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 comparisons of the peptide–bound PTH1R with and without G-protein coupling (ePTH–bound; PDB 6FJ3). b, d, Duration of cAMP signaling responses induced by PTH, ABL and LA-PTH analogs. c, e Interactions of the peptide residues (positions 5 and 11) with R_G and R₀ state PTH1R, respectively. Potential interactions of peptide agonists with R₀ state receptor were analyzed based on the template of ePTH-bound PTH1R. (PDB 6FJ3). Source data are provided as a Source Data file.