Figure 3.

Features of TG6 TCR bound to L^d-HF10 complex. (A) TCR footprint on the solvent-accessible surfaces of the L^d-HF10 complexes (L^d α1, cyan; L^d α2, magenta; peptide, white). The TCR CDR loops are colored as TCR footprint. Areas of TCR contact with pMHC (≤ 4.5Å) are colored as: CDR1α, red; CDR2α, blue; CDR3α, yellow; CDR1β, gray; CDR2β, orange; CDR3β green. (B-E), Interactions between TG6 CDRs and L^d-HF10. HF10 residues are shown in white carbon stick; residues on TG6 are shown in pale yellow carbon stick; residues of L^d are shown in magenta (α1) and cyan (α2) carbon stick; H-bonds and salt bridges are indicated by green lines. (B) Extensive contacts between TCR CDR3β and p7E of the HF10 peptide. (C) Residues of both TCR CDR3α and L^d contact HF10 p5V. (D) Hydrophobic stacking of TCR CDR3β and L^d with HF10 p8F. (E) Both TG6 CDR2β and CDR3β form a salt bridge to p9D. L^d also provides contacts. See Movie S2.