8cx4

TCR-antigen complex AS8.4-YEIH-HLA*B27

spinqualitylabelsall models 8cx4, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8cx4 is a 5 chain structure with sequence from Escherichia coli and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A3F718_HUMAN Involved in the presentation of foreign antigens to the immune system.[ARBA:ARBA00002297] Publication Abstract from PubMed Human leucocyte antigen B*27 (HLA-B*27) is strongly associated with inflammatory diseases of the spine and pelvis (for example, ankylosing spondylitis (AS)) and the eye (that is, acute anterior uveitis (AAU))(1). How HLA-B*27 facilitates disease remains unknown, but one possible mechanism could involve presentation of pathogenic peptides to CD8(+) T cells. Here we isolated orphan T cell receptors (TCRs) expressing a disease-associated public beta-chain variable region-complementary-determining region 3beta (BV9-CDR3beta) motif(2-4) from blood and synovial fluid T cells from individuals with AS and from the eye in individuals with AAU. These TCRs showed consistent alpha-chain variable region (AV21) chain pairing and were clonally expanded in the joint and eye. We used HLA-B*27:05 yeast display peptide libraries to identify shared self-peptides and microbial peptides that activated the AS- and AAU-derived TCRs. Structural analysis revealed that TCR cross-reactivity for peptide-MHC was rooted in a shared binding motif present in both self-antigens and microbial antigens that engages the BV9-CDR3beta TCRs. These findings support the hypothesis that microbial antigens and self-antigens could play a pathogenic role in HLA-B*27-associated disease. Autoimmunity-associated T cell receptors recognize HLA-B*27-bound peptides.,Yang X, Garner LI, Zvyagin IV, Paley MA, Komech EA, Jude KM, Zhao X, Fernandes RA, Hassman LM, Paley GL, Savvides CS, Brackenridge S, Quastel MN, Chudakov DM, Bowness P, Yokoyama WM, McMichael AJ, Gillespie GM, Garcia KC Nature. 2022 Dec;612(7941):771-777. doi: 10.1038/s41586-022-05501-7. Epub 2022 , Dec 7. PMID:36477533 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also MHC 3D structures MHC I 3D structures

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