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. 2021 Jun 24;12:3938. doi: 10.1038/s41467-021-23756-y

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© The Author(s) 2021

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 — a–c Representative snapshots showing the position of the lipid(s) in the three sites (active conformation) that were most occupied by PIP2 (a site 1; b site 2; c site 3). The residues interacting with the lipid within each of these sites are indicated (blue), the PIP2 molecules are reported in sticks colored according to the CG beads and the receptor backbone (active conformation) as a white surface. d FRET signal between Bodipy-FL PIP2 (2.5 molar%) and Lumi-4 Tb attached to C255^6.27 of the wild-type receptor or of the putative PIP2-binding sites mutants. The FRET signal obtained with negative control labeled lipid Bodipy-PA is given for comparison. The signal was normalized to that measured with wild-type GHSR. Data in (d) are mean ± SD of three experiments and is provided as a Source data file.