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J Biol Chem, Vol. 274, Issue 9, 5755-5761, February 26, 1999
From the Cancer Research Campaign Growth Factor Group, Department
of Biochemistry, University of Birmingham, Edgbaston,
Birmingham, B15 2TT, United Kingdom
Interleukin-11 (IL-11) is a member of the gp130
family of cytokines. These cytokines drive the assembly of multisubunit
receptor complexes, all of which contain at least one molecule of the
transmembrane signaling receptor gp130. A complex of IL-11 and the
IL-11 receptor (IL-11R) has been shown to interact with gp130, with
high affinity, and to induce gp130- dependent signaling. In this study,
we have identified residues crucial for the binding of murine IL-11
(mIL-11) to both the IL-11R and gp130 by examining the activities of
mIL-11 mutants in receptor binding and cell proliferation assays. The location of these residues, as predicted from structural studies and a
model of IL-11, reveals that mIL-11 has three distinct receptor binding
sites. These are structurally and functionally analogous to the
previously defined receptor binding sites I, II, and III of
interleukin-6 (IL-6). This supports the hypothesis that IL-11 signals
via the formation of a hexameric receptor complex and indicates that
site III is a generic feature of cytokines that signal via association
with gp130.
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