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J Biol Chem, Vol. 273, Issue 28, 17579-17584, July 10, 1998
From the Departments of Autophosphorylation of
Ca2+/calmodulin (CaM)-dependent protein
kinase II (CaM-kinase II) induces a striking >1,000-fold increase in
its affinity for CaM, which has been called CaM trapping. Two peptides
modeled after the CaM binding domain of CaM-kinase II were previously
shown to kinetically resemble CaM binding to phosphorylated and
dephosphorylated forms of the enzyme, thus providing a model system
with which to define the molecular basis of CaM trapping. In this
report, the specific contribution of each amino acid to the rates of
association and dissociation, and the overall Kd of
CaM binding to CaM-kinase II was determined using an overlapping peptide family, and a fluorescently labeled CaM. The association rate
constants were similar for the entire family of peptides and ranged
from 8 × 107 to 32 × 107
M
A Mechanism for Calmodulin (CaM) Trapping by CaM-kinase II
Defined by a Family of CaM-binding Peptides
,
Neurobiology and Anatomy,
¶ Internal Medicine, and Biochemistry and Molecular
Biology, The University of Texas Medical School at Houston,
Houston, Texas 77030
1 s1. In contrast, the
dissociation rate constants for the peptides varied by >3500-fold and
ranged from 0.26 to 7 × 105 s1. These
rate constants yield overall Kd values for binding CaM to the peptides that range from 2 × 109
M to 2 × 1013 M. Extending
the low affinity CaM-binding peptide, CKII(296-312), to include
293Phe-Asn-Ala295 provided the single largest
contribution to the decreased dissociation rate constant, 1,300-fold.
It was further shown using Ala-substituted peptides that the basic
residues 296Arg-Arg-Lys299 were also essential
for slow CaM dissociation; however, their contribution was realized
only when 293Phe-Asn-Ala295 were present. These
results suggest a plausible model in which autophosphorylation of
CaM-kinase II leads to a conformational change in the region of
293Phe-Asn-Ala295 which makes these residues
accessible for binding to CaM. As a consequence of these changes,
further CaM contacts with 296Arg-Arg-Lys299 are
established leading to high affinity CaM binding or "CaM trapping."
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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