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(Received for publication, September 14, 1994; and in revised form, November 21, 1994) The Ras-binding domain (RBD) of human Raf-1 was purified from Escherichia coli, and its interaction with Ras was
investigated. Its dissociation constant with
p21
Volume 270,
Number 7,
Issue of February 17, 1995 pp. 2901-2905
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
and the
Ras-binding Domain of the Human Raf-1 Protein Kinase
guanyl-5`-yl imidodiphosphate was found
to be 18 nM, with a slight preference for H-ras over K- and
N-ras. Oncogenic forms bind with slightly lower affinity. The affinity
of RBD for effector region mutants or the GDP-bound form of
p21 is in the micromolar range, which means that
100-fold lower affinity is not sufficient for signal transduction. The
rate of the GTPase of p21 is not modified by
RBD. Since P
release is found not to be rate limiting, the
Ras-Raf signal of the cell may be terminated by the intrinsic GTPase of
p21.
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