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 investig
ated using gel filtration and gel electrophoresis. A ternary complex b
etween IL-4 and the soluble domains of the two receptors was shown to
exist in solution. The association constant between gamma(c) and the s
table complex of IL-4/sIL-4R is in the millimolar range, making the te
rnary complex a feasible target for crystallization studies.