Direct evidence of a heterotrimeric complex of human interleukin-4 with its receptors

Protein Sci. 1995 Mar;4(3):382-6. doi: 10.1002/pro.5560040304.


The mode of binding of interleukin-4 (IL-4) to its two known receptors, specific receptor IL-4R and a shared receptor gamma c, was investigated using gel filtration and gel electrophoresis. A ternary complex between IL-4 and the soluble domains of the two receptors was shown to exist in solution. The association constant between gamma c and the stable complex of IL-4/sIL-4R is in the millimolar range, making the ternary complex a feasible target for crystallization studies.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Interleukin-4 / genetics
  • Interleukin-4 / metabolism*
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation
  • Receptors, Interleukin / genetics
  • Receptors, Interleukin / metabolism*
  • Receptors, Interleukin-4
  • Recombinant Proteins / metabolism
  • Sequence Analysis


  • Receptors, Interleukin
  • Receptors, Interleukin-4
  • Recombinant Proteins
  • Interleukin-4