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. 2023 Jan 23;14:376. doi: 10.1038/s41467-022-35726-z

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© The Author(s) 2023

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 Comparison of overall M2R structures of ACh-bound S1 (green), ACh-bound S2 (cyan), and Ixo-bound (orange, PDB: 4MQS) active states from the orthogonal, extracellular, and intracellular views. b, c Comparison of the P^5.50-V^3.40-F^6.44 core triad (b) and conserved side-chains R121^3.50, Y206^5.58, and Y440^7.53(c) in three different active conformations. d Comparison of ACh binding pockets in S1 and S2 states. Red arrow indicates the conformational differences for Y426^7.39. Black dashed lines indicate hydrogen-bond interactions with N404^6.52. e, f Density maps of residues in the orthosteric pocket in S1 (e) and S2 (f) states. The probable water molecule in S2 state is shown as red sphere. g Comparison of the TM2-TM7 interface between S1 and S2 state. Red arrow indicates the conformational differences for W427^7.40. h Comparison of the Ixo and ACh binding pockets in S1 state. Red arrow indicates different rotamers of W400^6.48. i Comparison of the toggle switch W400^6.48 conformations when bound to antagonist (PDB: 3UON), ACh, and Ixo.