title: [Structure and function of the essential light chain of myosin].
abstract: The review summarizes recent data on the structure and functions of the essential light chain of myosin. The essential light chain of myosin is known to stabilize the arm. Consistent with the model of the shift of the dynamic population of conformations, the conformational flexibility of the essential light chain of myosin is emphasized, which opens the way to the determination of its novel functions. The assumption is substantiated that the interaction between the C-terminal domain of the essential light chain and the N-terminal subdomain of the heavy chain of myosin is involved in the coupling of ATP hydrolysis and rotation of the arm. The recent data indicate that the isoforms of the essential light chain with the additional N-terminal peptide are capable of interacting with actin and the src-homologous domain 3 of myosin. The structural aspects of these interactions and the modulatory role of the isoforms of the essential light chain of myosin are discussed.
authors.forename: D S
authors.initials: DS
authors.lastname: Ushakov
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009119:Muscle Contraction; D018995:Myosin Heavy Chains / Q000737:chemistry; D018994:Myosin Light Chains / Q000737:chemistry* / Q000502:physiology; D011487:Protein Conformation; D020033:Protein Isoforms / Q000737:chemistry
chemical_list: D018994:Myosin Light Chains; D020033:Protein Isoforms; D018995:Myosin Heavy Chains