Structure of Leu-2/T8 as deduced from the sequence of a cDNA clone

Behring Inst Mitt. 1985 Aug:(77):48-55.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Antigens, Differentiation, T-Lymphocyte
  • Antigens, Surface* / genetics
  • Base Sequence
  • Biological Evolution
  • Cloning, Molecular
  • DNA / genetics
  • Genes
  • Humans
  • Immunoglobulin kappa-Chains / genetics
  • Membrane Proteins / genetics
  • Membrane Proteins / immunology
  • Protein Conformation
  • Recombination, Genetic
  • Solubility
  • T-Lymphocytes / physiology*

Substances

  • Antigens, Differentiation, T-Lymphocyte
  • Antigens, Surface
  • Immunoglobulin kappa-Chains
  • Membrane Proteins
  • DNA