Article
Structure/function analysis of the interaction of phosphatidylinositol 4,5-bisphosphate with actin-capping protein: implications for how capping protein binds the actin filament.
The Journal of biological chemistry - 23 Feb 2007
Kim Kyoungtae, McCully Michelle E, Bhattacharya Nandini, Butler Boyd, Sept David, Cooper John A
Abstract excerpt
The heterodimeric actin-capping protein (CP) can be inhibited by polyphosphoinositides, which may be important for actin polymerization at membranes in cells. Here, we have identified a conserved set of basic residues on the surface of CP that are important for the interaction with phosphatidylinositol 4,5-bisphosphate (PIP(2)). Computational docking studies predicted the identity of residues involved in this...
Topics
- Actin Capping Proteins
- Actins
- Animals
- Binding Sites
- Humans
- Models, Molecular
- Mutation
- Phosphatidylinositol 4,5-Diphosphate
- Protein Binding
- Protein Subunits