Structure of the complex between human T-cell receptor, viral peptide and HLA-A2

被引:0
|
作者
Garboczi, David N. [1 ,2 ]
Ghosh, Partho [1 ,2 ]
Utz, Ursula [3 ]
Fan, Qing R. [1 ,2 ]
Biddison, William E. [4 ]
Wiley, Don C. [1 ,2 ]
机构
[1] Harvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA
[2] Harvard Univ, Howard Hughes Med Inst, Cambridge, MA 02138 USA
[3] Inst Rech Clin Montreal, Immunol Lab, Montreal, PQ H2W 1R7, Canada
[4] NINDS, Mol Immunol Sect, Neuroimmunol Branch, NIH, Bethesda, MD 20892 USA
来源
JOURNAL OF IMMUNOLOGY | 2010年 / 185卷 / 11期
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中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Recognition by a T-cell antigen receptor (TCR) of peptide complexed with a major histo-compatibility complex (MHC) molecule occurs through variable loops in the TCR structure which bury almost all the available peptide and a much larger area of the MHC molecule. The TCR fits diagonally across the MHC peptide-binding site in a surface feature common to all class I and II MHC molecules, providing evidence that the nature of binding is general. A broadly applicable binding mode has implications for the mechanism of repertoire selection and the magnitude of alloreactions.
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页码:134 / 141
页数:8
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