Figure 1 - full size

 

Figure 1.
Figure 1. Crystal structure of scTCR–MAM–HLA-DR1/HA ternary complex. Lime, MAM; blue, DR1 ; cyan, DR1 ; red, HA; purple, TCR V ; green, TCR V . (a) Structure of the scTCR–MAM–HLA-DR1/HA complex. (b) Interaction surfaces of MAM and scTCR T7. Center, surface presentation of the MAM–scTCR structure; left, opened-up view of the MAM-binding surface of scTCR; right, opened-up view of the TCR-binding surface of MAM. Hydrophobic surface patches are colored in cyan. CDR and HV4 loops of TCR are shown as 'worms'. Selected aromatic residues of TCR at the interface are shown as rods. (c) Sequence alignment of the V residues of MAM-reactive (indicated by +) and unreactive (-) TCRs. Conserved or conservatively substituted residues (red boxes) and MAM-contacting residues (red asterisks) are indicated. (d) Sequence alignment of MAM-contacting residues of TCR V s that are most frequently activated by MAM (indicated by +) and TCR V s that are less frequently activated by MAM. Conserved residues indicated as in c; green boxes mark strictly conserved cysteine residues.

The above figure is reprinted by permission from Macmillan Publishers Ltd: Nat Struct Mol Biol (2007, 14, 169-171) copyright 2007.