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. 2022 May 24;8:50. doi: 10.1038/s41421-022-00412-3

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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 — a Detailed interactions of 5-CT with residues in the binding pocket of 5-HT_5A. b 2D schematic representation of interactions between 5-CT and residues in the ligand-binding pocket of 5-HT_5A, analyzed by LigPlot⁺ program. The polar interactions are indicated as black dashed lines. c Effects of alanine mutation of pocket residues of 5-HT_5A on 5-CT-induced G_i protein recruitment. Three independent NanoBiT assays in triplicates were performed. Each data point presents mean ± SEM from a representative experiment.