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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.
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