title: The interaction of cofilin with the actin filament.
abstract: Cofilin is a key actin-binding protein that is critical for controlling the assembly of actin within the cell. Here, we present the results of molecular docking and dynamics studies using a muscle actin filament and human cofilin I. Guided by extensive mutagenesis results and other biophysical and structural studies, we arrive at a model for cofilin bound to the actin filament. This predicted structure agrees very well with electron microscopy results for cofilin-decorated filaments, provides molecular insight into how the known F- and G-actin sites on cofilin interact with the filament, and also suggests new interaction sites that may play a role in cofilin binding. The resulting atomic-scale model also helps us understand the molecular function and regulation of cofilin and provides testable data for future experimental and simulation work.
authors.affiliation: Department of Biomedical Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA.
authors.forename: Diana Y
authors.initials: DY
authors.lastname: Wong
authors.forename: David
authors.initials: D
authors.lastname: Sept
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry* / Q000378:metabolism*; D000595:Amino Acid Sequence; D001665:Binding Sites; D051338:Cofilin 1 / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D011485:Protein Binding; D025941:Protein Interaction Mapping; D020836:Protein Structure, Quaternary; D017386:Sequence Homology, Amino Acid
chemical_list: D051338:Cofilin 1