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. 2019 Oct 8;9:14432. doi: 10.1038/s41598-019-51016-z

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© The Author(s) 2019

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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Signaling of PTH via the PTH1R is complex and triggers various signaling outcomes. (A) PTH binding to the PTH1R is bimodal and requires binding of the C-terminal fragment of the peptide to the extracellular domain of the receptor while the N-terminal part engages the transmembrane domain of the receptor. (B) Slight modifications of either the N- or C-termini of the peptides or introduction of a limited number of amino acid substitutions change the signaling outcome of the PTH1R. PTH-βArr is a modified bovine PTH, substitutions to the equivalent amino acid residue in human PTH are highlighted in orange, substitutions to a non-standard amino acid are shown in red. Abbreviations: dW, d-Tryptophan: nd, no data.