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. 2022 Jul 5;13:3872. doi: 10.1038/s41467-022-31443-9

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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 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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Fig. 3 — a The overview of the crystal structure of CO3 γδ TCR-CD1a-sulfatide is shown. Both chains of the CO3 γδ TCR (γ chain in green; δ chain in orange) docked on the side of CD1a (grey) - β2m (blue) heterodimer forming a ~90° incident angle. The lipid antigen sulfatide (yellow) protrudes from the cleft of CD1a. The sideways docking mode is contrasted with b CD1a-restricted autoreactive αβ TCR BK6 (α chain in coral, β chain in cyan, lipid ligand in dark green; PDB: 4X6C) and c the docking modes seen for MR1 restricted γδ TCRs: G7 (left: PDB 6MWR) and G83.C4 (right: 7LLI). MR1 is shown in black, γ chains are in green, δ chains in orange and the MR1 ligands in pink.