Ontology highlight
ABSTRACT:
SUBMITTER: O'Neall-Hennessey E
PROVIDER: S-EPMC3606567 | biostudies-literature | 2013 Mar
REPOSITORIES: biostudies-literature
Acta crystallographica. Section F, Structural biology and crystallization communications 20130222 Pt 3
All muscle-based movement is dependent upon carefully choreographed interactions between the two major muscle components, myosin and actin. Regulation of vertebrate smooth and molluscan muscle contraction is myosin based (both are in the myosin II class), and requires the double-headed form of myosin. Removal of Ca2+ from these muscles promotes a relatively compact conformation of the myosin dimer, which inhibits its interaction with actin. Although atomic structures of single myosin heads are a ...[more]