Abstract
The Tl/Leu-l/CD5 molecule, a human T-cell surface glycoprotein of relative molecular mass (Mr) 67,0001–3, has been implicated in the proliferative response of activated T cells4 and in T-cell helper function5. A similar involvement in T-cell proliferation has been reported for Ly-1 (refs 6–8), the murine homologue of T1 (ref. 9). Here we report the complete amino-acid sequence of the T1 precursor molecule deduced from complementary DNA clones. The protein contains a classical signal peptide; a 347-amino-acid extracellular segment; a transmembrane region; and a 93-amino-acid intracellular segment. The extracellular segment contains many cysteine residues and is composed of two related structural domains separated by a proline/threonine-rich region. The T1 molecule has structural features characteristic of other receptor molecules.
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Jones, N., Clabby, M., Dialynas, D. et al. Isolation of complementary DNA clones encoding the human lymphocyte glycoprotein T1/Leu-1. Nature 323, 346–349 (1986). https://doi.org/10.1038/323346a0
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DOI: https://doi.org/10.1038/323346a0
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