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. 2021 Feb 16;12:1074. doi: 10.1038/s41467-021-21016-7

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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. 5 — a Additional densities corresponding to annular (orange) and inter-subunit lipids (yellow). b Tentative modelling of cholesterol at annular lipid site with density shown in transparent orange (contoured at σ 2.0). Putative lipid–protein interactions are indicated with dashed lines. c Top view of the putative cholesterol density. d, f Superposition of apo-5HT₃R-Salipro and apo-5HT₃R-detergent (6BE1, chain C) d at the cholesterol-binding pocket viewed from the membrane or f at the Cys loop, β1-β2 loop, M2–M3 linker junction viewed from the neighbouring subunit. Part of the Cys loop (C135-D138) and the TMD are omitted for clarity. Distances are labelled in the same colour scheme as the structures. Density sharpened using RELION with auto-determined b-factor is shown in transparent grey for residues R218 and E53 (contoured at σ 6.0). e, g Same as d, f but showing a superposition of the serotonin-bound 5HT₃R-Salipro (chain C) and 5HT₃R-detergent (6DG8) structures. Density for residues R218 and E53 is contoured at σ 6.5.