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. 2017 Jul 28;7:6812. doi: 10.1038/s41598-017-07215-7

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© The Author(s) 2017

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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(A) Amino acid sequence of Transactive response DNA-binding protein 43 (TDP-43). The fragment of 102–269 (RRM12) used in this study is overlined. The amino acids, which are able to chelate zinc ions are highlighted: in light blue – Glu, in green – Cys and in grey – His. Image was generated using Protein Sequence Analysis Tool⁵⁴. (B) Domain organization of TDP-43: NTD – N-terminal domain; NLS – nuclear localization signal; RRM1 (106–177 a.a.) and RRM2 (192–259 a.a.) – RNA-recognition domains; NES – nuclear export signal.