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. 2020 Sep 21;10:15402. doi: 10.1038/s41598-020-72373-0

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© The Author(s) 2020

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Stereoscopic representation of the TSP2 D3 and D4 folds. The polypeptide chain is colored with a rainbow color scheme beginning with blue at the N-terminus and ending in red at the C-terminus of the entire molecule. (a) The D3 β-helix, indicating the two capping α-helices. (b) The D4 β-sandwich. The D4 α-helix is close to the C-terminus of the polypeptide chain and caps the D3 β-helix C-terminus, a feature unique to TSP2. The figure was generated using the computer program PyMol v1.8.0.2 (Schrödinger, LLC, https://www.pymol.org).