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. 2024 Apr 10;9:88. doi: 10.1038/s41392-024-01803-6

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© The Author(s) 2024

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 30 — a Schematic representation of the allosteric agonist PCO371 bound to PTH1R (PDB: 8GW8). b Detailed binding modes of PTH1R binding to PCO371. Hydrogen bonds are presented as orange dashes. c Superposition of the PTH1R bound to PCO371 (displayed in pink) and PTH (displayed in blue) reveals conformational changes upon PCO371 binding