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- W4319936563 abstract "The mechanism of T cell triggering upon antigen presentation remains a challenging problem. To observe structural and dynamics changes in the T cell receptor (TCR) upon binding of a peptide-MHC complex (pMHC), we carried out coarse grained molecular dynamics simulations of TCR-only and TCR-pMHC systems starting from a recently solved cryo-EM structure of the TCR and CD3 co-receptors. The simulations were performed in biological membranes for an aggregated length of 2 ms. We observed that, while unengaged TCRs adopted conformations in which the TCR extracellular domain is bent and the dynamics of the CD3 co-receptors is restricted, the pMHC-bound TCRs adopted elongated conformations that allowed CD3 co-receptors to diffuse more freely. We subsequently identified a pair of conserved glycines in the hinge region of the TCRβ. Simulations of mutated TCRs whose hinge regions were rigidified by substituting the glycines into prolines or alanines were less able to restrain the CD3 co-receptor chains. Consistently, we found that reporter cells containing TCRs with rigidified hinges were hyperresponsive to pMHC stimulation in the early (2-4 hour) phase of T cell activation. These results suggest a model where TCR triggering is facilitated by increased CD3 dynamics, which, in turn, is facilitated by TCR-pMHC engagement, rigidification of the TCR hinge, or both." @default.
- W4319936563 created "2023-02-11" @default.
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- W4319936563 date "2023-02-01" @default.
- W4319936563 modified "2023-10-17" @default.
- W4319936563 title "When the TCR's engaged, the CD3 epsilons will play: A dynamic T cell receptor (TCR) triggering mechanism" @default.
- W4319936563 doi "https://doi.org/10.1016/j.bpj.2022.11.1148" @default.
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