Figure 4 - full size

 

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).

The above figure is reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2000, 19, 5611-5624) copyright 2000.