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- W4387364216 abstract "Transglutaminase 3 (TG3), the autoantigen of dermatitis herpetiformis (DH), is a calcium dependent enzyme that targets glutamine residues in polypeptides for either transamidation or deamidation modifications. To become catalytically active TG3 requires proteolytic cleavage between the core domain and two C-terminal β-barrels (C1C2). Here, we report four X-ray crystal structures representing inactive and active conformations of human TG3 in complex with a TG3-specific Fab fragment of a DH patient derived antibody. We demonstrate that cleaved TG3, upon binding of a substrate-mimicking inhibitor, undergoes a large conformational change as a β-sheet in the catalytic core domain moves and C1C2 detaches. The unique enzyme-substrate conformation of TG3 without C1C2 is recognized by DH autoantibodies. The findings support a model where B-cell receptors of TG3-specific B cells bind and internalize TG3-gluten enzyme-substrate complexes thereby facilitating gluten-antigen presentation, T-cell help and autoantibody production." @default.
- W4387364216 created "2023-10-06" @default.
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- W4387364216 date "2023-10-05" @default.
- W4387364216 modified "2023-10-10" @default.
- W4387364216 title "Autoantibody binding and unique enzyme-substrate intermediate conformation of human transglutaminase 3" @default.
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- W4387364216 doi "https://doi.org/10.1038/s41467-023-42004-z" @default.
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