The Closed State of the Thin Filament Is Not Occupied in Fully Activated Skeletal Muscle.

ABSTRACT: Muscle contraction is powered by actin-myosin interaction controlled by Ca²⁺ via the regulatory proteins troponin (Tn) and tropomyosin (Tpm), which are associated with actin filaments. Tpm forms coiled-coil dimers, which assemble into a helical strand that runs along the whole ∼1 μm length of a thin filament. In the absence of Ca²⁺, Tn that is tightly bound to Tpm binds actin and holds the Tpm strand in the blocked, or B, state, where Tpm shields actin from the binding of myosin heads. Ca²⁺ binding to Tn releases the Tpm from actin so that it moves azimuthally around the filament axis to a closed, or C, state, where actin is partially available for weak binding of myosin heads. Upon transition of the weak actin-myosin bond into a strong, stereo-specific com

SUBMITTER: Bershitsky SY 

PROVIDER: S-EPMC5389958 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature