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

The mode of binding of interleukin‐4 (IL‐4) to its two known receptors, specific receptor IL‐4R and a shared receptor γc, 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 γc and the stable complex of IL‐4/sIL‐4R is in the millimolar range, making the ternary complex a feasible target for crystallization studies.

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