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- W2067067381 abstract "αβ T-cell receptors (TcRs) play a central role in cellular immune response. They are members of the Ig superfamily, with extracellular regions of the α and β chains each comprising a V-type domain and a C-type domain. We have determined the ectodomain structure of an αβ TcR, which recognizes the autoantigen myelin basic protein. The 2.0-Å-resolution structure reveals canonical main-chain conformations for the Vα, Vβ, and Cβ domains, but the Cα domain exhibits a main-chain conformation remarkably different from those previously reported for TcR crystal structures. The global IgC-like fold is maintained, but a piston-like rearrangement between BC and DE β-turns results in β-strand slippage. This substantial conformational change may represent a signaling intermediate. Our structure is the first example for the Ig fold of the increasingly recognized concept of “metamorphic proteins.”" @default.
- W2067067381 created "2016-06-24" @default.
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- W2067067381 date "2010-07-01" @default.
- W2067067381 modified "2023-09-26" @default.
- W2067067381 title "An Alternative Conformation of the T-Cell Receptor α Constant Region" @default.
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- W2067067381 doi "https://doi.org/10.1016/j.jmb.2010.05.053" @default.
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