Abstract
HLA-E binds specifically to MHC class Ia leader peptides in a TAP (transporter associated with antigen processing)-dependent manner. It interacts with CD94/NKG2A receptors on natural killer cells and this inhibits natural killer cell lysis of the cell displaying HLA-E. The crystal structure of HLA-E demonstrates that the specificity of leader peptide binding is a structurally defined intrinsic property of HLA-E.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Antigen Presentation*
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Antigens, CD / immunology*
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Antigens, CD / metabolism
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Cytotoxicity, Immunologic
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HLA Antigens / chemistry
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HLA Antigens / immunology*
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HLA Antigens / metabolism
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HLA-E Antigens
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Histocompatibility Antigens Class I / chemistry
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Histocompatibility Antigens Class I / immunology*
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Histocompatibility Antigens Class I / metabolism
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Killer Cells, Natural / immunology*
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Lectins, C-Type*
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Membrane Glycoproteins / immunology*
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Membrane Glycoproteins / metabolism
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Mice
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Models, Immunological
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NK Cell Lectin-Like Receptor Subfamily C
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NK Cell Lectin-Like Receptor Subfamily D
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Protein Sorting Signals / metabolism
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Receptors, Immunologic / immunology*
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Receptors, Immunologic / metabolism
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Receptors, Natural Killer Cell
Substances
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Antigens, CD
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HLA Antigens
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Histocompatibility Antigens Class I
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Klrc1 protein, mouse
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Klrd1 protein, mouse
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Lectins, C-Type
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Membrane Glycoproteins
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NK Cell Lectin-Like Receptor Subfamily C
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NK Cell Lectin-Like Receptor Subfamily D
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Protein Sorting Signals
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Q surface antigens
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Receptors, Immunologic
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Receptors, Natural Killer Cell