title: Molecular basis of myosin assembly: coiled-coil interactions and the role of charge periodicities.
abstract: Complementation of alternating zones of positive and negative charge in the myosin rod enables molecules to interact in a number of ways. This accounts for the complexity of the molecular organisation of thick filaments. However, directed mutagenesis of expressed LMM cDNA indicated that charge zone complementation is not a major driving force in myosin polymerisation. Instead, it probably serves to prevent unfavourable interaction geometries.
authors.affiliation: MRC Laboratory of Molecular Biology, Cambridge, England.
authors.forename: S J
authors.initials: SJ
authors.lastname: Atkinson
authors.forename: M
authors.initials: M
authors.lastname: Stewart
mesh_terms: D004563:Electrochemistry; D016296:Mutagenesis; D009218:Myosins / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D011487:Protein Conformation
chemical_list: D009218:Myosins