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PDBsum entry 2cik
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Immune system/peptide
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PDB id
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2cik
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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 structure of the human allo-Ligand hla-B3501 In complex with a cytochrome p450 peptide: steric hindrance influences tcr allo-Recognition.
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Authors
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C.S.Hourigan,
M.Harkiolaki,
N.A.Peterson,
J.I.Bell,
E.Y.Jones,
C.A.O'Callaghan.
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Ref.
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Eur J Immunol, 2006,
36,
3288-3293.
[DOI no: ]
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PubMed id
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Abstract
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Virus-specific T cell populations have been implicated in allo-recognition. The
subdominant T cell receptor JL12 recognizes both HLA-B*0801 presenting the
Epstein-Barr virus-derived peptide FLRGRAYGL and also HLA-B*3501 presenting the
cytochrome p450 self peptide KPIVVLHGY. This cross-reactivity could promote the
rejection of HLA-B*3501-positive cells in Epstein-Barr virus-exposed HLA-B*0801
recipients. LC13, the dominant TCR against the HLA-B*0801:FLRGRAYGL complex,
fails to recognize HLA-B*3501:KPIVVLHGY. We report the 1.75-Angstrom resolution
crystal structure of the human allo-ligand HLA-B*3501:KPIVVLHGY. Similarities
between this structure and that of HLA-B*0801:FLRGRAYGL may facilitate
cross-recognition by JL12. Moreover, the elevated peptide position in
HLA-B*3501:KPIVVLHGY would provide steric hindrance to LC13, preventing it from
interacting in the manner in which it interacts with HLA-B*0801:FLRGRAYGL. These
findings are relevant to understanding the basis of T cell cross-reactivity in
allo-recognition, optimal transplant donor-recipient matching and developing
specific molecular inhibitors of allo-recognition.
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