Article ID Journal Published Year Pages File Type
10802871 Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 2011 9 Pages PDF
Abstract
► CaM interaction with its target peptides depends on the number of Ca2+ bound. ► CaM-Ca interacts with the unphosphorylated DAPK CaM binding domain. ► CaM-Ca3 interacts with the phosphorylated DAPK CaM binding domain peptide. ► CaM with four Ca2+ is required for interaction with the EGFR CaM binding domain.
Keywords
Related Topics
Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
Preview
A general strategy to characterize calmodulin-calcium complexes involved in CaM-target recognition: DAPK and EGFR calmodulin binding domains interact with different calmodulin-calcium complexes
Authors
, , , , , , , , ,