Figure 3.
Figure 3 Interaction of TCR HA1.7 with HLA-DR1 and HA peptide.
(A) TCR contacts. Contacts of CDR residues (solid red lines)
with HLA-DR1 (solid blue lines) and the HA peptide (solid black
line) are indicated by dashed green and dashed red lines,
respectively. Human MHC class II conserved (filled circles) and
polymorphic residues (open circles) are shown. (B) Contacts
between CDR2 and
the conserved Lys39 of DR1 outside
of the peptide-binding site (van der Waals contacts, dashed
black lines; potential hydrogen bonds, dashed red lines). (C)
MHC–peptide solvent-accessible surface buried by the TCR,
colored by CDR type (see key). The total accessible surfaces
buried on pMHC by the TCR are 1111 Å^2 for HA1.7/DR1/HA,
1041 Å^2 for D10/I-Ak/CA, 1031 Å^2 for A6/A2/TAX,
918 Å^2 for B7/A2/TAX and 1111 Å^2 for
2C/H-2Kb/DEV8. The antigenic peptide is shown by a white line.
Figures were prepared with MOLSCRIPT (Kraulis, 1991), Raster3D
(Merritt and Murphy, 1994) and GRASP (Nicholls et al., 1991).
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
Embo J
(2000,
19,
5611-5624)
copyright 2000.
and
the conserved Lys39 of DR1 
outside
of the peptide-binding site (van der Waals contacts, dashed
black lines; potential hydrogen bonds, dashed red lines). (C)
MHC–peptide solvent-accessible surface buried by the TCR,
colored by CDR type (see key). The total accessible surfaces
buried on pMHC by the TCR are 1111 Å^2 for HA1.7/DR1/HA,
1041 Å^2 for D10/I-Ak/CA, 1031 Å^2 for A6/A2/TAX,
918 Å^2 for B7/A2/TAX and 1111 Å^2 for
2C/H-2Kb/DEV8. The antigenic peptide is shown by a white line.
Figures were prepared with MOLSCRIPT (Kraulis, 1991), Raster3D
(Merritt and Murphy, 1994) and GRASP (Nicholls et al., 1991).