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 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.
Hoffman
R C
RC
Immunex Corporation, Seattle, Washington 98101, USA.
Castner
B J
BJ
Gerhart
M
M
Gibson
M G
MG
Rasmussen
B D
BD
March
C J
CJ
Weatherbee
J
J
Tsang
M
M
Gustchina
A
A
Schalk-Hihi
C
C
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D015847:Interleukin-4 / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D018123:Receptors, Interleukin / Q000235:genetics / Q000378:metabolism*; D019948:Receptors, Interleukin-4; D011994:Recombinant Proteins / Q000378:metabolism; D017421:Sequence Analysis
D018123:Receptors, Interleukin; D019948:Receptors, Interleukin-4; D011994:Recombinant Proteins; D015847:Interleukin-4