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PDBsum entry 1kgc
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Immune system
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PDB id
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1kgc
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Contents |
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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 1.5 a crystal structure of a highly selected antiviral t cell receptor provides evidence for a structural basis of immunodominance.
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Authors
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L.Kjer-Nielsen,
C.S.Clements,
A.G.Brooks,
A.W.Purcell,
J.Mccluskey,
J.Rossjohn.
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Ref.
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Structure, 2002,
10,
1521-1532.
[DOI no: ]
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PubMed id
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Abstract
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Despite a potential repertoire of >10(15) alphabeta T cell receptors (TcR), the
HLA B8-restricted cytolytic T cell response to a latent antigen of Epstein-Barr
virus (EBV) is strikingly limited in the TcR sequences that are selected. Even
in unrelated individuals this response is dominated by a single highly
restricted TcR clonotype that selects identical combinations of hypervariable
Valpha, Vbeta, D, J, and N region genes. We have determined the 1.5 A crystal
structure of this "public" TcR, revealing that five of the six
hypervariable loops adopt novel conformations providing a unique combining site
that contains a deep pocket predicted to overlay the HLA B8-peptide complex. The
findings suggest a structural basis for the immunodominance of this clonotype in
the immune response to EBV.
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Figure 8.
Figure 8. Ball and Stick Stereo View Representation of the
Public Sequences Selected in the LC13 TcR b Chain and the
Residues with which They InteractThe CDR3b subdivided into three
regions according to the origin of the relevant codons: Vb
(red), Db and N (light blue), and Jb (green). The interacting
residues are color-coded yellow (Vb) and gray (Va). Structural
superposition of a region of the identical Jb segment from LC13
(green) and B7 (yellow) that highlights the conformational
differences.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2002,
10,
1521-1532)
copyright 2002.
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