 |
|
Title
|
 |
MARCKS, a major protein kinase C substrate, assumes non-helical conformations both in solution and in complex with Ca2+-calmodulin.
|
 |
|
Authors
|
 |
M.Matsubara,
E.Yamauchi,
N.Hayashi,
H.Taniguchi.
|
 |
|
Ref.
|
 |
Febs Lett, 1998,
421,
203-207.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
MARCKS, a major cellular substrate for protein kinase C, plays important roles
in various cellular functions and its functions are regulated by calmodulin. We
have studied the conformational properties of recombinant human MARCKS in
solution and in complex with calmodulin. Circular dichroism (CD) spectra showed
a high content of random coil in physiological solution. When MARCKS or
MARCKS-derived calmodulin-binding peptide was complexed with Ca2+-calmodulin,
little change was observed in the CD spectra, suggesting that MARCKS binds with
calmodulin in a non-helical conformation, which is unique among the
calmodulin-binding proteins.
|
 |
 |
 |