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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. 1 — a Cryo-EM density map of Xenopus KCNQ1-CaM (xKCNQ1-CaM), and its model structure (c). CaM is colored dark green and KCNQ1 subunits are in shades of red. b xKCNQ1-CaM in complex with ML277 and its model structure (d). CaM and ML277 are colored dark green and orange, respectively. KCNQ1 subunits are in shades of blue. Additional densities, likely representing unmodeled detergent or lipid molecules are shown in gray. For further analysis of these densities, see Supplementary Fig. 7. e Overall superposition of a single subunit of xKCNQ1-CaM and xKCNQ1-CaM-ML277 shows a visible twist in the C-helix coiled-coil domain (CTD). HA-HC refers to helices within the C-terminal domain of KCNQ1.