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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. 4 — a, c Superposition of xKCNQ1-CaM-ML277 structure (orange) onto the open pore hKCNQ1-CaM-KCNE3-PIP2 (PDB-ID: 6V01, green) via the S4-S5 linker and S5 helix. hKCNE3 is shown as pale green for comparison. c Side view of PIP2 tail and ML277. b, d Superposition of xKCNQ1-CaM-ML277 structure (orange) onto the modeled hKCNQ1-PIP2-ML277 structure (gray, PDB-ID: 6V01, KCNE3 was omitted). Binding free energy for ML277 was −54.5 ± 0.65 kcal/mol. d Side view of PIP2 tails and ML277. e Superposition of KCNE3 (green) from hKCNQ1-CaM-PIP2-KCNE3 (PDB-ID: 6V01), onto the xKCNQ1-CaM-ML277 complex (cyan and blue). f Conformations of T71 and F68 in KCNE3 and F270 in hKCNQ1 do not allow L266 to rotate and ML277 to bind. Residues on KCNQ1-CaM-PIP2-KCNE3 (green) are lime green and corresponding residues Leu256 and Phe260 in xKCNQ1-CaM-ML277 are shown in cyan. VDW surfaces of Leu256, Phe260 in xKCNQ1, and F270 in hKCNQ1 are shown as mesh to indicate potential clashes.