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. 2022 Jun 29;13:3760. doi: 10.1038/s41467-022-31526-7

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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. 6 — a, b Overview of published KCNQ-ligand binding plotted on the xKCNQ1-CaM-ML277 structure. Different isoform structures were aligned based on the pore-forming domain. a View from within the plane of the membrane. Cyan and blue for the two subunits comprising the ML277 binding pocket. b Top view from the extracellular side clipped at the level of the ML277/ML213/retigabine binding sites for clarity. c Superposition of hKCNQ4-CaM-ML213 (gray) onto xKCNQ1-CaM-ML277 (different shades of blue for different subunits, xKCNQ1 residue side chains shown in cyan) ML277 is shown in orange, and ML213 in black. Van der Waals surfaces indicate potential clashes. d Superposition of xKCNQ1-CaM-ML277 onto hKCNQ4-CaM-ML213 (ML213 in black and hKCNQ4 residue side chains in gray). Van der Waals surfaces indicate potential clashes between ML277 and hKCNQ4 residues W242, L306′ and V248′.