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. 2022 Sep 15;13:5417. doi: 10.1038/s41467-022-33121-2

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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. 2 — Binding pocket for ONO-0740556, viewed from the extracellular side (a) and membrane plane (b, c). ONO-0740556 and receptor residues involved in agonist binding are shown as orange and blue sticks, respectively. The dashed lines indicate hydrogen bonds. d Schematic representation of the interactions between ONO-0740556 and the receptor within 4.5 Å. e NanoBiT-G-protein dissociation assays for LPA₁ and its mutants. Concentration–response curves for ONO-074055-dependent G-protein dissociation signals for LPA₁ are shown as means ± s.e.m. from three independent experiments. To match the expression of LPA₁-WT to those of mutants with lower expression, 1:5 volume [WT (1:5)] plasmid was used. Source data are provided as a Source Data file. It should be noted that mutations of these head phosphate group-recognizing residues enhanced the G-protein dissociation in high concentration of the agonist, while the reason is uncertain. f Conservation of the ONO-0740556 binding site in LPA_1–6.