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. 2023 May 3;617(7960):417–425. doi: 10.1038/s41586-023-06030-7

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© The Author(s) 2023

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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Extended Data Fig. 3 — a. The positive effect of additional D138^3.32N mutation on the momSalB-mediated cAMP inhibition through KOR. The additional D138^3.32N mutation does not rescue U50,488 or GR89,696-mediated cAMP inhibition. Data are grouped data ± s.e.m. from n = 3 biological replicates. Full quantitative parameters from this experiment are listed in Supplementary Table 10. b. Effects of mutations in the hydrophobic pocket on the binding affinity of momSalB. Data are grouped data ± s.e.m. from n = 3 independent biological replicates. Full quantitative parameters from this experiment are listed in Supplementary Table 11. c and d. Chemical structures of SalB, momSalB, and EOM-SalB. Differences are highlighted by red colour. The agonist activity of each analogue is shown in the parentheses. Data for EOM-SalB was taken from ref. ¹⁹. Binding poses of SalB and EOM-SalB at KOR were revealed by molecular docking performed in the Schrodinger Maestro v12.9. The three ligands occupy a similar binding pocket with different extents toward the hydrophobic pocket.