Abstract
Autoimmune diseases are caused by self-reactive lymphocytes that have escaped deletion. Here we have determined the structure of the trimolecular complex for a T cell receptor (TCR) from a patient with multiple sclerosis that causes autoimmunity in transgenic mice. The structure showed a TCR topology notably different from that of antimicrobial TCRs. Rather than being centered on the peptide-major histocompatibility complex, this TCR contacted only the N-terminal peptide segment and made asymmetrical interactions with the major histocompatibility complex helices. The interaction was dominated by the hypervariable complementarity-determining region 3 loops, indicating that unconventional topologies are possible because of the unique complementarity-determining region 3 sequences created during rearrangement. This topology reduces the interaction surface with peptide and alters the geometry for CD4 association. We propose that unusual TCR-binding properties can permit autoreactive T cells to escape deletion.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Autoantigens / chemistry
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Autoantigens / immunology*
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Autoimmunity / immunology*
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CD4 Antigens / chemistry
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CD4 Antigens / metabolism
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Complementarity Determining Regions / immunology
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Crystallography, X-Ray
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Epitopes / chemistry
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Epitopes / immunology
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Histocompatibility Antigens Class II / chemistry*
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Histocompatibility Antigens Class II / immunology*
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Humans
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Models, Molecular
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Molecular Sequence Data
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Myelin Basic Protein / chemistry
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Myelin Basic Protein / immunology
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Peptide Fragments / chemistry
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Peptide Fragments / immunology
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Peptides / chemistry
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Peptides / immunology*
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Protein Structure, Tertiary
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Receptors, Antigen, T-Cell / chemistry*
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Receptors, Antigen, T-Cell / immunology*
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Structure-Activity Relationship
Substances
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Autoantigens
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CD4 Antigens
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Complementarity Determining Regions
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Epitopes
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Histocompatibility Antigens Class II
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Myelin Basic Protein
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Peptide Fragments
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Peptides
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Receptors, Antigen, T-Cell
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myelin basic protein 83-99