Structure of Leu-2/T8 as deduced from the sequence of a cDNA clone.
We have determined the primary structure of the Leu-2/T8 T lymphocyte differentiation antigen from the complete nucleotide sequence of a cDNA clone. The protein consists of a classical signal peptide, two external protein domains, a hydrophobic transmembrane segment, and a highly charged intracytoplasmic tail. The N-terminal external domain of the mature protein is homologous to immunoglobulin and T cell receptor variable regions. Protein structural predictions suggest that this domain can indeed fold like an immunoglobulin domain. The Leu-2/T8 protein has no segment that is homologous to a constant region. However, the membrane-proximal domain appears to serve as a hinge. These studies indicate that Leu-2/T8 is another member of the immunoglobulin supergene family.
D000595:Amino Acid Sequence; D000945:Antigens, Differentiation, T-Lymphocyte; D000954:Antigens, Surface / Q000235:genetics; D001483:Base Sequence; D005075:Biological Evolution; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D005796:Genes; D006801:Humans; D007145:Immunoglobulin kappa-Chains / Q000235:genetics; D008565:Membrane Proteins / Q000235:genetics / Q000276:immunology; D011487:Protein Conformation; D011995:Recombination, Genetic; D012995:Solubility; D013601:T-Lymphocytes / Q000502:physiology*
D000945:Antigens, Differentiation, T-Lymphocyte; D000954:Antigens, Surface; D007145:Immunoglobulin kappa-Chains; D008565:Membrane Proteins; D004247:DNA