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Molecular Characterization of the Murine Cytotoxic T-Cell Membrane Glycoprotein Ly-3 (CD8)
Michael Panaccio, Matthew T. Gillespie, Ian D. Walker, Louis Kirszbaum, Jennifer A. Sharpe, Glen H. Tobias, Ian F. C. McKenzie and Nicholas J. Deacon
Proceedings of the National Academy of Sciences of the United States of America
Vol. 84, No. 19 (Oct. 1, 1987), pp. 6874-6878
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/30683
Page Count: 5
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The murine Ly-2/3 glycoprotein is a surface marker of T cells restricted by class I major histocompatibility complex antigens. It is a disulfide-bonded heterodimer in which either the α or α ′ polypeptide chain encoded by Ly-2 is covalently linked to the β polypeptide chain encoded by Ly-3. The nucleotide and predicted amino acid sequence of the murine Ly-3 cDNA, isolated by using the rat Ly-3 cDNA clone pX9.15, together with the amino acid sequence of Ly-3.1 peptides and the N terminus, are presented here. The alignment of peptide data from the Ly-3.1 antigen with that of the predicted amino acid sequence of the Ly-3.2 antigen confirmed that the putative Ly-3 cDNA clones do in fact encode the Ly-3 protein. The Ly-3.2 cDNA clones encode a protein of 213 amino acids, which includes a 21-residue leader sequence and structural features in common with immunoglobulin variable, joining, and hinge regions. Searches of protein data bases revealed that Ly-3 is a member of the immunoglobulin superfamily with significant homology to Ly-2, immunoglobulin variable region κ and λ light chains, and the β chain of the T-cell receptor. A single N-linked glycosylation site was found at asparagine-13. The relative expression of two mRNA species (approximately 1.3 and 2.3 kilobases) varied according to the source of mRNA. A murine B1 repeat was located in the 3′ untranslated region of Ly-3 cDNA clones.
Proceedings of the National Academy of Sciences of the United States of America © 1987 National Academy of Sciences