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- W2017310933 abstract "The T cell receptor (TCR) together with accessory cluster of differentiation 3 (CD3) molecules (TCR–CD3 complex) is a key component in the primary function of T cells. The nature of association of the transmembrane domains is of central importance to the assembly of the complex and is largely unknown. Using multiscale molecular modeling and simulations, we have investigated the structure and assembly of the TCRα–CD3ε–CD3δ transmembrane domains both in membrane and in micelle environments. We demonstrate that in a membrane environment the transmembrane basic residue of the TCR closely interacts with both of the transmembrane acidic residues of the CD3 dimer. In contrast, in a micelle the basic residue interacts with only one of the acidic residues. Simulations of a recent micellar nuclear magnetic resonance structure of the natural killer (NK) cell-activating NKG2C–DAP12–DAP12 trimer in a membrane further indicate that the environment significantly affects the way these trimers associate. Since the currently accepted model for transmembrane association is entirely based on a micellar structure, we propose a revised model for the association of transmembrane domains of the activating immune receptors in a membrane environment." @default.
- W2017310933 created "2016-06-24" @default.
- W2017310933 creator A5003973067 @default.
- W2017310933 creator A5035246521 @default.
- W2017310933 date "2013-02-01" @default.
- W2017310933 modified "2023-10-03" @default.
- W2017310933 title "An Atomistic Model for Assembly of Transmembrane Domain of T cell Receptor Complex" @default.
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- W2017310933 doi "https://doi.org/10.1021/ja308413e" @default.
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