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. 2018 Feb 26;8:3643. doi: 10.1038/s41598-018-22033-1

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© The Author(s) 2018

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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Sodium Channel Schematic Diagram. Domain III and Domain IV, along with their inter-linker and the CTD, regulate channel function and calcium sensitivity. DIII-DIV linker contains the fast inactivation “particle” (IFM motif). DIV-S6 contains the putative drug-binding residue, F1760, which is key for Ranolazine binding. The enlarged CTD contains six α-helices which aggregate to form an intact domain for calmodulin binding. Calmodulin (CaM) binds to the IQ-domain (α₆) under low cytosolic calcium conditions (structure adapted from Chagot et al., 2009 and Gabelli et al., 2014). E1784K may rearrange CTD structure affecting Calmodulin interaction with other channel sites, such as the DIII-DIV linker.