Published online 17 January 2006 doi:10.1084/jem.20051886
Rockefeller University Press, 0022-1007 $8.00
JEM, Volume 203, Number 1, 47-52
Stoichiometry of the murine 
T cell receptor
Sandra M. Hayes and
Paul E. Love
Laboratory of Mammalian Genes and Development, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892
CORRESPONDENCE Sandra M. Hayes: hayessa{at}upstate.edu
The T cell receptor for antigen (TCR) complex is organized into two functional domains: the antigen-binding clonotypic heterodimer and the signal-transducing invariant CD3 and TCR
chains. In most vertebrates, there are two different clonotypic heterodimers (TCR
ß and TCR
) that define the
ß and 
T cell lineages, respectively.
ß- and 
TCRs also differ in their invariant chain subunit composition, in that
ßTCRs contain CD3
and CD3
dimers, whereas 
TCRs contain only CD3
dimers. This difference in subunit composition of the
ß- and 
TCRs raises the question of whether the stoichiometries of these receptor complexes are different. As the stoichiometry of the murine 
TCR has not been previously investigated, we used two quantitative immunofluorescent approaches to determine the valency of TCR
heterodimers and CD3
dimers in surface murine 
TCR complexes. Our results support a model of murine 
TCR stoichiometry in which there are two CD3
dimers for every TCR
heterodimer.

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