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PDBsum entry 1nez
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Immune system
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PDB id
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1nez
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Contents |
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274 a.a.
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99 a.a.
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122 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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The crystal structure of a tl/cd8alphaalpha complex at 2.1 a resolution: implications for modulation of t cell activation and memory.
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Authors
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Y.Liu,
Y.Xiong,
O.V.Naidenko,
J.H.Liu,
R.Zhang,
A.Joachimiak,
M.Kronenberg,
H.Cheroutre,
E.L.Reinherz,
J.H.Wang.
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Ref.
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Immunity, 2003,
18,
205-215.
[DOI no: ]
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PubMed id
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Abstract
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TL is a nonclassical MHC class I molecule that modulates T cell activation
through relatively high-affinity interaction with CD8alphaalpha. To investigate
how the TL/CD8alphaalpha interaction influences TCR signaling, we characterized
the structure of the TL/CD8alphaalpha complex using X-ray crystallography.
Unlike antigen-presenting molecules, the TL antigen-binding groove is occluded
by specific conformational changes. This feature eliminates antigen
presentation, severely hampers direct TCR recognition, and prevents TL from
participating in the TCR activation complex. At the same time, the
TL/CD8alphaalpha interaction is strengthened through subtle structure changes in
the TL alpha3 domain. Thus, TL functions to sequester and redirect CD8alphaalpha
away from the TCR, modifying lck-dependent signaling.
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Figure 1.
Figure 1. Overall View of the TL/CD8##Com-
plex Structure in Ribbon Drawing Prepared
with MOLSCRIPT (Krulis, 1991)
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Figure 2.
Figure 2. TL-Specific Amino Acid Residues
that Seal the ``Antigen Binding Groove'' in TL
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The above figures are
reprinted
by permission from Cell Press:
Immunity
(2003,
18,
205-215)
copyright 2003.
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