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The Extracellular Domain of the -Chain Is Essential for TCR Function

Basel Institute for Immunology, Basel, Switzerland

The -chain homodimer is a key component in the TCR complex and exerts its function through its cytoplasmic immunoreceptor-tyrosine activation motif (1). The -chain extracellular (EC) domain is highly conserved; however, its functional and structural contributions to the TCR signaling have not been elucidated. We show that the EC domain of the homodimer is essential for TCR surface expression. To gain a more detailed structural and functional information about the -chain EC domain, we applied a cysteine scanning mutagenesis to conserved amino acids of the short domain. The results showed that the interchain disulfide bridge can be displaced by seven or eight amino acids along the EC domain. The TCR signaling efficacy was dramatically reduced during peptide/MHC engagement in the mutants containing the displaced disulfide bond. These signaling defective mutants produced an unconventional early tyrosine phosphorylation pattern. While the tyrosine phosphorylated forms of (p21 and p23) could be observed during Ag stimulation, downstream signaling events such as the generation of phospho-p36, higher m.w. forms of phospho-, and phospho-/ZAP-70 complexes were impaired. Together these results suggest an important function of the phylogenetically conserved -EC domain.

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