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Figure 2.
Figure 2. The Orientations of TCR Docked on Class I MHC Are
Not Conserved to DiagonalThe orientation of AHIII 12.2 docking
is most orthogonal when compared to other TCR/pMHC structures
and Vα positions fall into two distinct groups. Class I MHC
from TCR/pMHC cocrystal structures were superimposed onto
p1049/A2 bound to AHIII 12.2. Molecular surfaces of the Vα and
Vβ domains from those TCR are shown in addition to the variable
domains of AHIII 12.2 (green) in order to compare the
orientations of the TCR on the MHC. (A) 2C (red), (B) KB5-C20
(light blue), (C) A6 (dark blue), (D) B7 (gold), (E) BM3.3
(cyan), and (F) LC13 (magenta). (G) JM22 (yellow). (H) The
positions of the center of mass of each TCR Vα and Vβ domain
are given pseudo-atoms and the positions connected by a line to
demonstrate the orientation that each TCR docks onto the MHC.
The different TCR are colored as in (A)–(G). The p1049/A2
complex is shown as a molecular surface representation with the
peptide colored yellow. (I) The orientation of Vα/Vβ pairs of
TCR docking on class II MHC compared to AHIII 12.2. HA1.7 is
shown in dark blue and D10 in light blue. AHIII 12.2 is shown in
green. (A)–(I) were constructed with Grasp (Nicholls et al.,
1991).
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