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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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Ranolazine docked to Na_V1.5-Na_VPas. The side view of Na_V1.5-Na_VPas homology model is shown docked to Ranolazine. The enlarged inset shows the cartoon structure of the drug binding to the central domains of the channel. The aromatic F1760 residue is outlined. Below the inset is a 3D-structure of Ranolazine (Nitrogen is blue, Oxygen is red, Carbon is green, and Hydrogen is grey). Conserved residues in DIII-DIV linker and CTD between Na_V1.5 and Na_VPas are indicated by a red asterisk.