Direct evidence of a heterotrimeric complex of human interleukin-4 with its receptors. |
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Authors: | R. C. Hoffman B. J. Castner M. Gerhart M. G. Gibson B. D. Rasmussen C. J. March J. Weatherbee M. Tsang A. Gustchina C. Schalk-Hihi et al. |
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Affiliation: | R. C. Hoffman, B. J. Castner, M. Gerhart, M. G. Gibson, B. D. Rasmussen, C. J. March, J. Weatherbee, M. Tsang, A. Gustchina, C. Schalk-Hihi, et al. |
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Abstract: | 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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Keywords: | interleukin-4 interleukin-4 receptor interleukin-2 receptor γ-chain stoichiometry |
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