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PDBsum entry 3gsn
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Immune system
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PDB id
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3gsn
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Contents |
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274 a.a.
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100 a.a.
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199 a.a.
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243 a.a.
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References listed in PDB file
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Key reference
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Title
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Structural bases for the affinity-Driven selection of a public tcr against a dominant human cytomegalovirus epitope.
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Authors
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S.Gras,
X.Saulquin,
J.B.Reiser,
E.Debeaupuis,
K.Echasserieau,
A.Kissenpfennig,
F.Legoux,
A.Chouquet,
M.Le gorrec,
P.Machillot,
B.Neveu,
N.Thielens,
B.Malissen,
M.Bonneville,
D.Housset.
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Ref.
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J Immunol, 2009,
183,
430-437.
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PubMed id
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Abstract
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Protective T cell responses elicited along chronic human CMV (HCMV) infections
are sometimes dominated by CD8 T cell clones bearing highly related or identical
public TCR in unrelated individuals. To understand the principles that guide
emergence of these public T cell responses, we have performed structural,
biophysical, and functional analyses of an immunodominant public TCR (RA14)
directed against a major HLA-A*0201-restricted HCMV Ag (pp65(495-503)) and
selected in vivo from a diverse repertoire after chronic stimulations. Unlike
the two immunodominant public TCRs crystallized so far, which focused on one
peptide hotspot, the HCMV-specific RA14 TCR interacts with the full array of
available peptide residues. The conservation of some peptide-MHC
complex-contacting amino acids by lower-affinity TCRs suggests a shared
TCR-peptide-MHC complex docking mode and supports an Ag-driven selection of
optimal TCRs. Therefore, the emergence of a public TCR of an oligoclonal
Ag-specific response after repeated viral stimulations is based on a receptor
displaying a high structural complementarity with the entire peptide and
focusing on three peptide hotspots. This highlights key parameters underlying
the selection of a protective T cell response against HCMV infection, which
remains a major health issue in patients undergoing bone marrow transplantation.
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