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MARCKS, a major protein kinase C substrate, assumes non‐helical conformations both in solution and in complex with Ca 2+ ‐calmodulin
Author(s) -
Matsubara Mamoru,
Yamauchi Emiko,
Hayashi Nobuhiro,
Taniguchi Hisaaki
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01557-3
Subject(s) - marcks , calmodulin , circular dichroism , protein kinase a , random coil , substrate (aquarium) , protein kinase c , chemistry , biophysics , biochemistry , phosphorylation , biology , enzyme , ecology
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 Ca 2+ ‐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.