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Protein Science, Vol 4, Issue 3 382-386, Copyright © 1995 by Cold Spring Harbor Laboratory Press

ARTICLE

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

R. C. HOFFMAN, B. J. CASTNER, M. GERHART, M. G. GIBSON, B. D. RASMUSSEN, C. J. MARCH, M. G. WEATHERBEE, M. TSANG, A. GUSTCHINA, C. SCHALK-HIHI, L. RESHETNIKOVA and A. WLODAWER
Immunex Corporation, Seattle, Washington 98101 Present address: ZymoGenetics Inc., 1201 Eastlake Avenue East, Seattle, Washington 98102.

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.
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