title: Myosin structure, allostery, and mechano-chemistry.
abstract: Aberrant actomyosin interactions contribute to a wide range of pathophysiological conditions including heart failure, neurodegenerative disorders, and tumor growth. Despite surgical, interventional, and pharmacological advances, the burden and economic impact of these diseases remains immense. The initiation and progression of these disorders is frequently found to be a direct consequence of aberrant motile activity, which makes the in-depth investigation of the molecular mechanisms underlying actomyosin-dependent motility a prerequisite for the development of innovative treatment strategies. The present review describes key structural features of the actomyosin system, the basis of chemo-mechanical and allosteric coupling in the myosin motor domain, and molecular engineering and small molecule-based approaches to alter myosin function.
authors.affiliation: Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover, Germany; Centre for Structural Systems Biology, German Electron Synchrotron (DESY), 22607 Hamburg, Germany.
authors.forename: Matthias
authors.initials: M
authors.lastname: Preller
authors.forename: Dietmar J
authors.initials: DJ
authors.lastname: Manstein
mesh_terms: D000199:Actins / Q000737:chemistry / Q000502:physiology; D000494:Allosteric Regulation; D000818:Animals; D001665:Binding Sites; D006801:Humans; D009119:Muscle Contraction; D009218:Myosins / Q000737:chemistry* / Q000502:physiology; D054730:Protein Interaction Domains and Motifs; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary
chemical_list: D000199:Actins; D009218:Myosins