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. 2019 Nov 1;9:15864. doi: 10.1038/s41598-019-52436-7

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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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Modeling of wild-type and mutant DNAH6. Molecular structures of wild-type and mutant DNAH6 proteins were modeled with SWISS-MODEL software based on the template of dynein heavy chain, cytoplasmic (3vkh.pdb). (a,b) Structures of wild-type and mutant DNAH6 proteins; β-sheets (red arrows) are altered compared to the wild-type protein. (c,d) Enlarged view of the Asp-2194 site in wild-type and mutant DNAH6 protein. (e,f) Enlarged view of the Gly-3753 site in wild-type and mutant DNAH6 protein. Both Asp2194Glu and Gly3753Asp mutations of DNAH6 altered the structure of the protein. The positions of mutations are highlighted in blue.