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. 2017 Apr 26;7:1210. doi: 10.1038/s41598-017-01264-8

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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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Molecular Modeling of the TGF-β1/TβR-I/TβR-II/GAG System. (A) Docking results for HA463′ dp4 (top 50 solutions, in blue sticks) to TGF-β1/TβR-II (top) and TGF-β1/TβR-II/TβR-I (bottom). TGF-β1 is shown in yellow, TβR-II in green and TβR-I in grey. The part of the system not used for docking calculations (TβR-I and TβR-II on the right side of TGF-β1) is depicted with transparency. (B) Zoomed view of the residue Lys40 of TβR-I (in thick sticks, carbons in cyan) that interacts with the negatively charged groups of HA463′ dp4 (in thick sticks, carbons in orange). Protein is shown in cartoon.