Conformational changes linked to ADP release from human cardiac myosin bound to actin-tropomyosin.

ABSTRACT: Following binding to the thin filament, β-cardiac myosin couples ATP-hydrolysis to conformational rearrangements in the myosin motor that drive myofilament sliding and cardiac ventricular contraction. However, key features of the cardiac-specific actin-myosin interaction remain uncertain, including the structural effect of ADP release from myosin, which is rate-limiting during force generation. In fact, ADP release slows under experimental load or in the intact heart due to the afterload, thereby adjusting cardiac muscle power output to meet physiological demands. To further elucidate the structural basis of this fundamental process, we used a combination of cryo-EM reconstruction methodologies to determine structures of the human cardiac actin-myosin-tropomyosin filament complex at better

SUBMITTER: Doran MH 

PROVIDER: S-EPMC9859928 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature