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. 2019 Nov 7;9:16272. doi: 10.1038/s41598-019-52655-y

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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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Schematic presentation of the structures of the recombinant proteins generated in this study. (A) Domain structure and oligomerisation state of the generated recombinant full-length TSP-2 (trimer), TSP-4 and COMP (pentamers). Schematic representation adapted by permission from Springer Nature, Cell Mol Life Sci, Structures of thrombospondins, Carlson, C. B., Lawler, J. & Mosher, D. F., Copyright (2008)³⁹. All recombinant TSPs have been expressed with an N-terminal double strep II-tag and contain glycan side-chains which are not shown for reasons of clarity. (B) Structure of α₂δ-1 FL protein (adapted from Cell 139, Eroglu, Ç. et al., Gabapentin receptor αδ2δ-1 is a neuronal thrombospondin receptor responsible for excitatory CNS synaptogenesis, 380–392, Copyright (2009), with permission from Elsevier⁷) and simplified depiction of the derived non-proteolytically processed α₂δ-1 mutants generated in this study. The RRR motif, the von Willebrand Factor type A domain, and the glycan side-chains are not shown in the α₂δ-1 mutants for reasons of clarity.