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. 2022 Feb 8;12:2061. doi: 10.1038/s41598-022-06073-2

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© The Author(s) 2022

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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SV analyses of the interactions of TSP3 with partner TSPs (A) The c(s) distribution profile of a mixture containing 1.5 μM each of TSP1, TSP2 and TSP3 shows no interactions between these proteins. (B) The c(s) distribution profile of 5 μM each of TSP4-N₃₃₅ and TSP3 shows no association between the two proteins. (C) The c(s) distribution profile of 5 μM each of TSP4-N₃₃₅, TSP1 and TSP3 revealed no association between TSP3 and the TSP1:TSP4-N₃₃₅ binary complex. (D) The SV profile of 1.5 μM each of TSP4-N₃₃₅, TSP2 and TSP3 shows a ternary complex formation. (E) The c(s) distribution profile of 3 μM TSP4-N₃₃₅, 2.5 μM TSP2 and 3 μM TSP3_156-627 shows no ternary complex when the TSP3 head is absent. (F) The SV profile of a mixture containing 3.1 µM TSP4-N₂₅₃, 2.5 µM TSP2 and 2.5 µM TSP3 shows that TSP3 does not bind to the TSP2:TSP4-N₂₅₃ binary complex lacking the TSP4 XD1 domain.