Fig. 4: Comparison of TCR footprints on p53R175H–HLA-A2. | Nature Communications

Fig. 4: Comparison of TCR footprints on p53R175H–HLA-A2.

From: Structural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen

Fig. 4: Comparison of TCR footprints on p53R175H–HLA-A2.The alternative text for this image may have been generated using AI.

a Positions of CDR loops of TCR 12-6 on p53R175H–HLA-A2 (top view). CDRs of 12-6 are shown as numbered green (CDR1α, CDR2α, and CDR3α) or violet (CDR1β, CDR2β, and CDR3β) loops. HLA-A2 is depicted as a light blue surface. The p53R175H peptide is drawn in orange in stick representation with the mutated P8 His residue in cyan. The green and violet spheres mark the positions of the conserved intrachain disulfide of the Vα and Vβ domains, respectively. The red dashed line indicates the crossing angle of TCR to pMHC. b Positions of CDR loops of TCR 38-10 on p53R175H–HLA-A2 (top view). c Positions of CDR loops of TCR 1a2 on p53R175H–HLA-A2 (top view). d Footprint of TCR 12-6 on p53R175H–HLA-A2. The top of the MHC molecule is depicted as a light blue surface. The areas contacted by individual CDR loops are color-coded: CDR1α, dark green; CDR2α, cyan; CDR3α, light green; CDR1β, orange; CDR2β, red; CDR3β, pink. e Footprint of TCR 38-10 on p53R175H–HLA-A2. f Footprint of TCR 1a2 on p53R175H–HLA-A2.

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