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. 2019 Dec 19;20:200. doi: 10.1186/s12881-019-0937-1

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© The Author(s). 2019

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. 4 — Protein modeling of type X collagen (α1) NC1 domain and stylized structure of collagen X. a and b As illustrated in the ribbon protein model, both of the novel mutations are located in the NC1 domain of type X collagen (α1). One of the substitutions (p.Phe589Ile) affects a hydrophobic area and the other (p.Lys616Glu) is predicted to affect the surface of the assembled trimer. c The stylized structure of type X collagen (α1) is composed of a 18 amino acid signal peptide (S) and a 463 amino acid collagenous domain (HELIX) flanked by a 38-residue NC2 domain and a 161-residue NC1 domain. Furthermore, changes in the present study and most previous variants (Additional file 1) are located in NC1 domain