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. 2020 Feb 14;11:885. doi: 10.1038/s41467-020-14728-9

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© The Author(s) 2020

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. 4 — a Negatively charged environment of the ligand-binding pocket in FPR2 and docked fMLF peptide. b Molecular details of the ligand-binding pocket in FPR2 for fMLF. c Positively charged environment of the ligand-binding pocket in FPR1 and docked fMLF peptide. d Molecular details of the ligand-binding pocket in FPR1 for fMLF. Hydrogen-bonding interactions are shown as dashed lines. e Effects of mutations R205A and R201A on fMLFII-induced receptor activation determined by ³⁵S-GTPγS binding assays (left) and BRET-based assays (right). BRET-based assays measured G_i coupling to receptors. n = 3–10, data are mean ± s.e.m. Source data are provided as a Source Data file.