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. 2017 Apr 20;15:78. doi: 10.1186/s12967-017-1180-1

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© The Author(s) 2017

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 3 — Structure modeling of the mutated domains of Desmin and Myopalladin. a The model of DES built from the segment of 149th–253th amino-acids sequence. The mutation caused the 234th acidic residue glutamic acid to be replaced by an alkaline residue lysine, which influence the dimerization of protein. b The model of MYPN built from the segment of 944th–1044th amino-acids sequence. The mutation caused the 989th liphatic amino-acid arginine to be replaced by a heterocyclic residue histidine in mutated myopallin, which changed the protein conformation and was predicted to influence the myopalladin interaction with ACTN