Structure of the complex between human T-cell receptor, viral peptide and HLA-A2.
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.
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
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Garboczi
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Ghosh
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Utz
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Fan
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Biddison
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Wiley
D018360:Crystallography, X-Ray; D016356:Gene Products, tax / Q000737:chemistry* / Q000276:immunology; D015789:HLA-A2 Antigen / Q000737:chemistry* / Q000276:immunology; D015368:Human T-lymphotropic virus 1 / Q000737:chemistry / Q000276:immunology; D006801:Humans; D007108:Immune Tolerance; D007128:Immunoglobulin Fragments / Q000737:chemistry; D008285:Major Histocompatibility Complex; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011948:Receptors, Antigen, T-Cell / Q000737:chemistry* / Q000276:immunology; D015398:Signal Transduction
D016356:Gene Products, tax; D015789:HLA-A2 Antigen; D007128:Immunoglobulin Fragments; D011948:Receptors, Antigen, T-Cell