The T-cell antigen receptor binds antigen in association with a cell surface molecule encoded by the major histocompatibility complex (MHC)1. MHC restricted recognition of antigen by this receptor leads to the complex pattern of programmed gene expression that characterizes T-cell activation. The eventual understanding of human T-cell function will require the complete elucidation of the structure of the human T-cell antigen receptor. On human T cells, clonally determined, disulphide-linked α and β chains of the receptor are non-covalently and stoichiometrically associated with three additional polypeptides known as the T3 complex2,3. These receptor subunits are glycoproteins of relative molecular mass (Mr) 25,000 (25K) and 20K (γ and δ) and a non-glycosylated 20K protein (ε). Our studies of murine T cells show that the mouse T-cell antigen receptor consists of at least seven distinct polypeptide chains4–6. In addition to clonotypic α and β chains, the murine complex consists of glycoproteins of 26K and 21K and endoglycosaminidase F (endo F)-insensitive polypeptides of 25K, 21K and 16K. The latter, which we have termed ζ (zeta), exists as a homodimer within the complex. The 26K component (gp26) has been shown to be the murine analogue of the human δ chain6,7. Other cross species homologies remain to be established, however none of the described human receptor components appear similar to the murine ζ polypeptide. We report here the use of an antiserum raised against the murine ζ subunit to identify a previously unrecognized component of the human T-cell antigen receptor. This human protein is T-cell specific and biochemically similar to the murine ζ polypeptide.
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Weissman, A., Samelson, L. & Klausner, R. A new subunit of the human T-cell antigen receptor complex. Nature 324, 480–482 (1986). https://doi.org/10.1038/324480a0
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