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J. Exp. Med.,
Volume 186, Number 11, December 1, 1997 1933-1938
Chain Constant Region
By
From the Basel Institute for Immunology, CH-4005 Basel, Switzerland
A single amino acid residue, Gln136, located within the connecting peptide domain of C
controls the ability of the 
/ TCR to transmit a full signal. TCRs in which this C residue is
mutated to Phe, the residue found in TCR-
, are unresponsive to antigenic ligands. Interestingly, this C residue is either polar or charged in every species studied thus far, including the
trout and the skate. In contrast, the analogous residue in C is always hydrophobic. In spite of
their compromised antigen responsiveness, the mutant TCR complex contains the CD3-, -
,
-
, and -
chains, and undergoes chain phosphorylation and ZAP-70 recruitment. However,
the biological response of the mutant TCR could be rescued with a calcium ionophore, implying that mutant TCRs are defective in generating a calcium-mediated signal. The implications
of the differences between C and C are considered.
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