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.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Electrophoresis, Polyacrylamide Gel
-
Humans
-
Interleukin-4 / genetics
-
Interleukin-4 / metabolism*
-
Molecular Sequence Data
-
Protein Binding
-
Protein Conformation
-
Receptors, Interleukin / genetics
-
Receptors, Interleukin / metabolism*
-
Receptors, Interleukin-4
-
Recombinant Proteins / metabolism
-
Sequence Analysis
Substances
-
Receptors, Interleukin
-
Receptors, Interleukin-4
-
Recombinant Proteins
-
Interleukin-4