Abstract
Recognition by a T-cell antigen receptor (TCR) of peptide complexed with a major histocompatibility 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 class 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.
Publication types
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Comment
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Crystallography, X-Ray
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Gene Products, tax / chemistry*
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Gene Products, tax / immunology
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HLA-A2 Antigen / chemistry*
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HLA-A2 Antigen / immunology
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Human T-lymphotropic virus 1 / chemistry
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Human T-lymphotropic virus 1 / immunology
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Humans
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Immune Tolerance
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Immunoglobulin Fragments / chemistry
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Major Histocompatibility Complex
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Models, Molecular
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Protein Binding
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Protein Conformation
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Receptors, Antigen, T-Cell / chemistry*
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Receptors, Antigen, T-Cell / immunology
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Signal Transduction
Substances
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Gene Products, tax
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HLA-A2 Antigen
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Immunoglobulin Fragments
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Receptors, Antigen, T-Cell