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Figure 4.
Figure 4 Recognition of the HA peptide by TCR HA1.7. (A) Binding
of the HA peptide (yellow) to the surface of the TCR HA1.7 (top)
and in the groove of DR1 (bottom). HA1.7 and DR1 were moved
apart and rotated around the long axis of the peptide by
-20° and +20°, respectively, in order to allow a better
view into the peptide-binding sites. Positive and negative
electrostatic surface potentials of HA1.7 and DR1 are indicated
in blue and red, respectively. (B) van der Waals contacts and
potential hydrogen bonds between TCR HA1.7 and HA peptide are
shown by black and red dashed lines, respectively. (C)
Electrostatic interactions between the three lysines (P–1, P3
and P8) of HA with acidic residues of HA1.7 TCR. (D) HA and CA
peptide residues that are contacted by TCR HA1.7 and D10,
respectively, are shown in red. The number of peptide residues
that are contacted by the different TCRs and the range over
which they are distributed are indicated. (A–C) were prepared
with MOLSCRIPT (Kraulis, 1991), Raster3D (Merritt and Murphy,
1994) and GRASP (Nicholls et al., 1991).
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