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• W2022987420 abstract "The interaction of the T cell receptor for antigen (TCR) with its antigen-major histocompatibility complex ligand is difficult to study because both are cell surface multimers. The TCR consists of two chains (alpha and beta) that are complexed to the five or more nonpolymorphic CD3 polypeptides. A soluble form of the TCR was engineered by replacing the carboxyl termini of alpha and beta with signal sequences from lipid-linked proteins, making them susceptible to enzymatic cleavage. In this manner, TCR heterodimers can be expressed independently of the CD3 polypeptides and in significant quantities (0.5 milligram per week). This technique seems generalizable to biochemical and structural studies of many other cell surface molecules as well." @default.
• W2022987420 created "2016-06-24" @default.
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• W2022987420 date "1990-08-10" @default.
• W2022987420 modified "2023-09-27" @default.
• W2022987420 title "Expression of T Cell Antigen Receptor Heterodimers in a Lipid-Linked Form" @default.
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• W2022987420 doi "https://doi.org/10.1126/science.1696397" @default.
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