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. 2017 Aug 15;7:8223. doi: 10.1038/s41598-017-08344-9

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© The Author(s) 2017

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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(a) Dose-response relations for quinine in cells expressing point-mutated and native ggTas2r1 constructs. The y-axis shows the relative fluorescence changes (ΔF/F), and the x axis the ligand concentration in μM. Green checks indicate residues involved in the binding, red crosses residues that are not involved in the binding, based on experimental data. (b) Involvement of residues K86, F89, N93, F181, L185, Y244, N247, and L251 in binding modes of quinine in the representative poses obtained with PELE simulations: the cell is colored in blue if the residue is found to interact with the ligand and in red if there is no interaction. The predicted agonist-bound conformation, pose 7 model 1, is marked by a green frame.