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. 2022 Aug 18;13:4862. doi: 10.1038/s41467-022-32594-5

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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. 3 — a A single-subunit alignment of GlyR-0.1gly and GlyR-0.1gly-THC structures highlighting the overall conformational changes associated with THC binding (left). Putty representation of pairwise root mean square deviation (RMSD) for the GlyR-0.1gly and GlyR-0.1gly-THC structures (right). The gray box points out regions that show most positional differences. b A close-up view of the alignment of GlyR-0.1gly and GlyR-0.1gly-THC structure showing rotameric rearrangement of residues in the vicinity of the THC binding site. c A comparison of the inter-subunit (gray dots) and intra-subunit (pink dots) cavities in GlyR-0.1gly (left) and GlyR-0.1gly-THC (right) predicted using F pocket algorithm⁷². The cavities predicted on the surface were removed for clarity.