title: Tropomyosin: double helix from the protein world.
abstract: This review concerns the structure and functions of tropomyosin (TM), an actin-binding protein that plays a key role in the regulation of muscle contraction. The TM molecule is a dimer of α-helices, which form a coiled-coil. Recent views on the TM structure are analyzed, and special attention is concentrated on those structural traits of the TM molecule that distinguish it from the other coiled-coil proteins. Modern data are presented on TM functional properties, such as its interaction with actin and ability to move on the surface of actin filaments, which underlies the regulation of the actin-myosin interaction upon contraction of skeletal and cardiac muscles. Also, part of the review is devoted to analysis of the effects of mutations in TM genes associated with muscle diseases (myopathies) on the structure and functions of TM.
authors.affiliation: Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia. levitsky@inbi.ras.ru
authors.forename: I A
authors.initials: IA
authors.lastname: Nevzorov
authors.forename: D I
authors.initials: DI
authors.lastname: Levitsky
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism; D000818:Animals; D006801:Humans; D009119:Muscle Contraction; D009132:Muscles / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D009928:Organ Specificity; D011485:Protein Binding; D011487:Protein Conformation; D020033:Protein Isoforms / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D055550:Protein Stability; D014335:Tropomyosin / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology
chemical_list: D020033:Protein Isoforms; D014335:Tropomyosin