Molecular cloning of cDNA encoding human interleukin-2 receptor

Nature. 1984 Oct;311(5987):631-5. doi: 10.1038/311631a0.

Abstract

The human interleukin-2 (IL-2) receptor was purified by affinity chromatography using the anti-Tac monoclonal antibody, and its N-terminal amino acid sequence was determined. Complementary DNA clones were isolated and sequenced to reveal the primary structure of the IL-2 receptor precursor, which has 272 amino acid residues. The receptor is separated into two domains by a putative 19-residue transmembrane region. Two mRNAs (1.4 and 3.5 kilobases) hybridizing to the cDNA clone were found in human T cells bearing the IL-2 receptor. The cDNA directed synthesis of the IL-2 receptor in COS cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular*
  • DNA / isolation & purification
  • DNA / metabolism*
  • DNA Restriction Enzymes
  • Genes*
  • Genetic Vectors
  • Humans
  • Nucleic Acid Hybridization
  • Protein Biosynthesis
  • RNA, Messenger / genetics
  • Receptors, Antigen, T-Cell / genetics*
  • Receptors, Immunologic / genetics*
  • Receptors, Immunologic / isolation & purification
  • Receptors, Interleukin-2
  • Transcription, Genetic

Substances

  • RNA, Messenger
  • Receptors, Antigen, T-Cell
  • Receptors, Immunologic
  • Receptors, Interleukin-2
  • DNA
  • DNA Restriction Enzymes

Associated data

  • GENBANK/X01057
  • GENBANK/X01058
  • GENBANK/X01402