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. 2019 Dec 17;9:19307. doi: 10.1038/s41598-019-55806-3

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© The Author(s) 2019

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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Views of ShK. (a) Overall structure of ShK, colored from blue at the N-terminus to red at the C-terminus, using the PDB file 4LFQ¹⁴. The six cystines are indicated, plus three residues thought to interact with the Kv1.3 potassium channel (Lys22, Tyr23 and Arg24). (b) Closeup view of the C17-C32 disulfide. The structures shown are iterations 200 from the molecular dynamics simulations, with the ground-state (negative χ₃) in green, and the alternative conformation (positive χ₃) in cyan. (c) End-on view of helix 21–24, showing the positions of Lys22, Tyr23 and Arg24 in iterations 200 from the molecular dynamics simulations. The Cys17-Cys32 disulfide is just visible at the back of the helix at the bottom.