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. 2019 Jan 30;9:973. doi: 10.1038/s41598-018-37801-2

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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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A missense change in the canine ALPL gene. (a) Sequence chromatograms of the ALPL c.1301T > G variant in exon 11 and a schematic representation of the ALPL gene. (b) Structure of the TNSALP polypeptide and multiple sequence alignment of the variant position in 18 mammalian species. Amino acid residues that make up the active site and the homodimerization interface are scattered along the polypeptide chain, whereas the calcium binding site and the crown domain form separate entities³⁴. The p. V434G missense change is located within the crown domain. Those amino acid residues that contain HPP-associated variants in humans are marked on top of the alignment and highlighted in grey (http://www.sesep.uvsq.fr/03_hypo_mutations.php). (c) Side and top views of the three-dimensional (3D) structure of the TNSALP homodimer, modelled from the crystal structure of the human placental alkaline phosphatase³². The two monomers are separated by different colours. The Val⁴³⁴ position is denoted with yellow, the active site residues with red and the collagen binding motif with black. The crown domain forms a flexible loop structure on top of the homodimer.