Insulin-like growth factor II receptor as a multifunctional binding protein

Nature. 1987 Sep;329(6137):301-7. doi: 10.1038/329301a0.


The primary structure of human insulin-like growth factor II receptor, predicted from the complementary DNA sequence, reveals a transmembrane receptor molecule with a large extracellular domain made up of fifteen repeat sequences and a small region homologous to the collagen-binding domain of fibronectin. The structural and biochemical features of the IGF-II receptor appear identical to those of the cation-independent mannose-6-phosphate receptor.

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
  • Animals
  • Base Sequence
  • Carrier Proteins
  • DNA / genetics
  • DNA, Recombinant
  • Humans
  • Membrane Proteins
  • Oocytes / metabolism
  • Rats
  • Receptor, IGF Type 2
  • Receptor, Insulin* / biosynthesis
  • Receptor, Insulin* / genetics
  • Receptor, Insulin* / isolation & purification
  • Receptors, Somatomedin
  • Repetitive Sequences, Nucleic Acid
  • Sequence Homology, Nucleic Acid
  • Xenopus laevis


  • Carrier Proteins
  • DNA, Recombinant
  • Membrane Proteins
  • Receptor, IGF Type 2
  • Receptors, Somatomedin
  • DNA
  • Receptor, Insulin