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Structural interactions of calmodulin with peptide from calmodulin binding regions of various enzymes
Author(s) -
Duangkham Yay,
Spratt Donald,
Dieckmann Thorsten,
Guillemette J. Guy
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.890.7
Subject(s) - calmodulin , linker , enzyme , biochemistry , chemistry , peptide , population , binding site , calcium binding protein , nitric oxide synthase , microbiology and biotechnology , biophysics , calcium , biology , demography , organic chemistry , sociology , computer science , operating system
Calmodulin (CaM) is an important calcium (Ca 2+ ) sensor in the cell and is able to activate over three hundred proteins to initiate cellular activities. CaM is a highly dynamic protein with a flexible central linker region joining the N‐terminal and C‐terminal domains. In each domain are two Ca 2+ binding sites that cause structural changes to CaM when Ca 2+ binds. These changes include the CaM central linker elongating and methionine rich hydrophobic patches being exposed, allowing for CaM to bind to the large population of target proteins. The structural interaction of CaM to short peptides from the CaM binding region of various target enzymes were investigated, including the nitric oxide synthase (NOS) enzyme.