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PDBsum entry 1lp9
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Immune system
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PDB id
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1lp9
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Contents |
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275 a.a.
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100 a.a.
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194 a.a.
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237 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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A correlation between tcr valpha docking on mhc and cd8 dependence: implications for t cell selection.
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Authors
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J.Buslepp,
H.Wang,
W.E.Biddison,
E.Appella,
E.J.Collins.
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Ref.
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Immunity, 2003,
19,
595-606.
[DOI no: ]
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PubMed id
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Abstract
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T cell receptors (TCR) adopt a similar orientation when binding with major
histocompatibility complex (MHC) molecules, yet the biological mechanism that
generates this similar TCR orientation remains obscure. We show here the
cocrystallographic structure of a mouse TCR bound to a human MHC molecule not
seen by the TCR during thymic development. The orientation of this xenoreactive
murine TCR atop human MHC deviates from the typical orientation more than any
previously determined TCR/MHC structure. This unique orientation is solely due
to the placement of the TCR Valpha domain on the MHC. In light of new
information provided by this structure, we have reanalyzed the existing TCR/MHC
cocrystal structures and discovered unique features of TCR Valpha domain
position on class I MHC that correlate with CD8 dependence. Finally, we propose
that the orientation seen in TCR recognition of MHC is a consequence of
selection during T cell development.
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Figure 1.
Figure 1. The Structure of AHIII 12.2 Bound to Xenogeneic
p1049/A2The stereo view of AHIII 12.2 TCR is depicted as a
ribbon (Carson, 1987) in magenta (α chain) and blue (β chain).
The A2 heavy chain is silver, β[2]m is cyan, and the p1049
peptide is gold.
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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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The above figures are
reprinted
by permission from Cell Press:
Immunity
(2003,
19,
595-606)
copyright 2003.
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