Fig. 7: Antigen specificity on HLA-DR4 towards T cell receptors.
Detailed interactions of SE residues with P4-Cit and (a) A03 TCR, (b) A07 TCR, (c) RA2.7 TCR, and (d) M134 TCR. Black dash represents a hydrogen bond and beige dash represent vdW interaction. e Top: Peptide sequences of α-eno-15cit10-22, Fibβ-74cit69-81 and Vim-64cit59-71 from pocket 1 to pocket 9. Bottom: The overlay of α-eno-15cit10-22 (orange), Fibβ-74cit69-81 (yellow), and Vim-64cit59-71 (pink) peptides from ternary complex structure. f Overlaid N-terminal region (P1-P4 position) of α-eno-15cit10-22 (orange), Fibβ-74cit69-81 (yellow), and Vim-64cit59-71 (pink) peptides and interactions with TCRs (A03 in red, and RA2.7 in orange). g Overlaid C-terminal region (P5-P9 position) of α-eno-15cit10-22 (orange), Fibβ-74cit69-81 (yellow), and Vim-64cit59-71 (pink) peptides and interactions with CDR3β of RA2.7 TCR. h Overlaid pHLA structures of α-eno-15cit10-22 (orange), Fibβ−74cit69-81 (yellow), and Vim-64cit59-71 (pink) ternary complexes. The deviation in α2 helix of the peptide antigen binding cleft was highlighted and measured (unit in \({\text{\AA}}\)). i The affinity analysis of A03 TCR, RA2.7 TCR and M134 TCR for HLA-DR4 with Vim-64cit59-71, α-eno-15cit10-22V20G, and Fibβ−74cit69-81 epitopes. All data were derived from three independent measurements with maximal TCR concentrations of 100 \(\mu\)M (n = 3). For each concentration the points represent the mean and error bars correspond to SD. RU denotes response units. Source data are provided as a Source Data file.
