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. 2017 Oct 13;7:13169. doi: 10.1038/s41598-017-13709-1

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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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Three-dimensional representation of the molecular docking of homology modelled wheat ATI CM3 (green ribbon) onto human TLR4-MD2 complex (grey ribbon). For better clarity of ATI-TLR4 complex visualization, MD2 molecule was removed after docking procedure. Black box highlights the oligopeptides constituting the discontinuous ATI binding interface. Oligopeptides are visualized as sticks (Panel A). Predicted cleavage sites by pepsin on wheat ATI CM3 (Panel B). The oligopeptides constituting the discontinuous ATI binding interface are highlighted in green. Residues constituting signal peptide (excluded from docking procedure) are highlighted in light blue.