Interactions Between CD2 and T-Cell Receptor Isoforms in CTL Function

  • Shigeo Koyasu
  • Ellis L. Reinherz


The recognition of specific target cells by cytotoxic T lymphocytes (CTL) involves a set of cell surface proteins. The physical interaction of a T-cell receptor (TCR) with a nominal peptide antigen bound to a specific major histocompatibility complex (MHC) molecule confers specificity on the CTL. The clonally unqiue antigen-specific binding component has been termed Ti and exists as a disulfide-linked Tiα-β heterodimer on the majority of peripheral T cells, although approximately 5% of T cells express Tiγ-δheterodimers (Meuer et al., 1984a; Marrack and Kappler, 1987; Brenner et al., 1988; Davis and Bjorkman, 1988; Raulet, 1989). The immunoglobulin-like Ti structure is noncovalently associated in a molecular complex with the CD3 subunits γ, δ, ε, ζ, and η, the latter molecules being involved in signal transduction (Clevers et al., 1988; Ashwell and Klausner, 1990; Koyasu et al., 1991a). The TCR has therefore been referred to as the CD3-Ti complex.


Major Histocompatibility Complex Cell Antigen Receptor Signal Transduction Function Sheep Erythrocyte Receptor CD3e Subunit 
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Copyright information

© Birkhäuser Boston 1993

Authors and Affiliations

  • Shigeo Koyasu
  • Ellis L. Reinherz

There are no affiliations available

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