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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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Visualization of the predicted epitope of ECD- scFvhFc on the PTH1R-ECD and the sequence diversity of β-arrestin-biased PTH variants highlights the complexity of PTH signaling. (A) The epitope of ECD- scFvhFc was determined using HDX-MS and is located in the α1 helix of the PTH1R-ECD (highlighted in light green). (B) Residues in the PTH1R-ECD interacting with ePTH (an engineered PTH used for structure determination (Ehrenmann et al., 2018, PDB 6FJ3) and overlapping with the putative epitope of ECD- scFvhFc are shown as light green sticks and numbered in three letter amino acid code (light green). Amino acids in ePTH interacting with these residues are shown as purple sticks and labeled using single letter amino acid code (purple). (C) Summary of the signaling behavior of PTH in the presence of ECD-scFvhFc. (D) Alignments of PTH, PTH related peptide (PTHrP) and β-arrestin-antagonizing variants. Abbreviations: Bpa, p-benzoylphenylalanine.