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. 2017 Aug 21;7:8953. doi: 10.1038/s41598-017-09518-1

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© The Author(s) 2017

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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Structures of different TRAIL polypeptides. (a) Three recombinant soluble forms of human TRAIL have been used in this study: a native TRAIL comprised of the extracellular domain of TRAIL, a dimeric TRAIL-Fc comprised of extracellular TRAIL domain fused to human IgG1 Fc domain, and a TRAIL-Trimer comprised of extracellular TRAIL domain fused to Trimer-Tag. Amino acid sequence lengths are shown for each protein and domain respectively. (b) Theoretical molecular weights (kDa) of both monomeric and multimeric forms of native TRAIL, TRAIL-Fc and TRAIL-Trimer, respectively. Native TRAIL associates into a non-covalently-linked homotrimer, TRAIL-Fc forms a covalently-linked homodimer, and TRAIL-Trimer forms a covalently-linked homotrimer.