Abstract
A novel translocation step is inferred from structural studies of the interactions between the intracellular calcium receptor protein calmodulin (CaM) and one of its regulatory targets. A mutant of CaM missing residues 2-8 (ΔNCaM) binds skeletal muscle myosin light chain kinase with high affinity but fails to activate catalysis. Small angle x-ray scattering data reveal that ΔNCaM occupies a position near the catalytic cleft in its complex with the kinase, whereas the native protein translocates to a position near the C-terminal end of the catalytic core. Thus, CaM residues 2-8 appear to facilitate movement of bound CaM away from the vicinity of the catalytic cleft.
Original language | English (US) |
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Pages (from-to) | 4535-4538 |
Number of pages | 4 |
Journal | Journal of Biological Chemistry |
Volume | 276 |
Issue number | 7 |
DOIs | |
State | Published - Feb 16 2001 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology