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. 2019 Nov 21;9:17291. doi: 10.1038/s41598-019-53756-4

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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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Structural homology modeling analysis. For (a–d) homology models that use the atomic coordinates of the MAGE peptide/HLA-A2 pMHC in complex with a Vβ5 TCR (5BRZ). Hydrophobic patches on the space-filling surface model are labeled green; charged and neutral surfaces white. For A, C and D, a ribbon cartoon shows where Vα normally binds to Vβ in the TCR α/β dimer. The intersection between the hydrophobic surface and the α/β contact surface was calculated and is shown in Å². (a) MAGE-A3 svd TCR homology modeled on 5BRZ template without the TCRα subunit. (b) MAGE-A3 svd TCR homology modeled on 5BRZ template after 100 nsec molecular dynamics simulation. (c) TRBV28 domain from previously crystalized TCR (6AT6) homology model on 5BRZ template without the TCRα subunit. (d) TRBV9 domain from previously crystalized TCR (6AVG) homology model on 5BRZ template without the TCRα subunit.