Extended Data Fig. 3: Overviews of the structures of the 302TIL TCR with the HHATp8F neoepitope and WT peptide-HLA-A*02:06 complexes.
From: Structural dissimilarity from self drives neoepitope escape from immune tolerance
a, Electron density (2Fo-Fc, 1σ) of the CDR loops in the neoepitope complex. b, Overview of the neoepitope ternary complex. The top shows the TCR variable domains, peptide, and the peptide-MHC binding groove (TCR constant domains, β2m, and the HLA-A*02:06 α3 domain are not shown). The bottom shows the positioning of the TCR over the peptide-MHC, with the spheres indicating the centers of mass of the Vα and Vβ domains. The TCR crossing and incident angles are indicated. c, Contact matrices for the 302TIL TCR-neoepitope-HLA-A*02:06 complex. Contacting amino acids are shown, with contacts defined as interatomic distances ≤ 4 Å. The numbers in each cell give the number of interatomic contacts for each amino acid pair; cells are colored according to the number of contacts, from white (minimum) to green (maximum). Red outlines indicate the presence of at least one hydrogen bond or salt-bridge. d–f, As in panels a–c except for the complex with the WT peptide.
