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• W2084612387 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." @default.
• W2084612387 created "2016-06-24" @default.
• W2084612387 creator A5006962892 @default.
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• W2084612387 date "2005-04-10" @default.
• W2084612387 modified "2023-10-13" @default.
• W2084612387 title "Unconventional topology of self peptide–major histocompatibility complex binding by a human autoimmune T cell receptor" @default.
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• W2084612387 doi "https://doi.org/10.1038/ni1187" @default.
• W2084612387 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3415330" @default.
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• W2084612387 hasPublicationYear "2005" @default.
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