Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
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作者:
Garboczi, David N.
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Harvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA
Harvard Univ, Howard Hughes Med Inst, Cambridge, MA 02138 USAHarvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA
Garboczi, David N.
[1
,2
]
Ghosh, Partho
论文数: 0引用数: 0
h-index: 0
机构:
Harvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA
Harvard Univ, Howard Hughes Med Inst, Cambridge, MA 02138 USAHarvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA
机构:
Harvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA
Harvard Univ, Howard Hughes Med Inst, Cambridge, MA 02138 USAHarvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA
机构:
Harvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA
Harvard Univ, Howard Hughes Med Inst, Cambridge, MA 02138 USAHarvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA
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
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.