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Direct evidence of a heterotrimeric complex of human interleukin‐4 with its receptors
Author(s) -
Hoffman Ross C.,
Castner Beverly J.,
Gerhart Mary,
Gibson Marylou G.,
Rasmussen Brian D.,
March Carl J.,
Weatherbee James,
Tsang Monica,
Gustchina Alla,
SchalkHihi Céline,
Reshetnikova Ludmila,
Wlodawer Alexander
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560040304
Subject(s) - heterotrimeric g protein , receptor , chemistry , ternary complex , size exclusion chromatography , chromatography , biochemistry , g protein , enzyme
The mode of binding of interleukin‐4 (IL‐4) to its two known receptors, specific receptor IL‐4R and a shared receptor γ 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 γ 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.