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Skeletal muscle alpha-actin is the principal protein component of the adult skeletal muscle thin filament. The interaction between skeletal muscle alpha-actin and the various myosin heavy chain proteins in the different muscle fibre types generates the force of muscle contraction. Skeletal muscle
ClC-1 protein channels facilitate rapid passage of chloride ions across cellular membranes, thereby orchestrating skeletal muscle excitability. Malfunction of ClC-1 is associated with myotonia congenita, a disease impairing muscle relaxation. Here, we present the cryo-electron microscopy (cryo-EM)
Uniquely, the ClC family harbours dissipative channels and anion/H(+) transporters that share unprecedented functional characteristics. ClC-1 channels are homodimers in which each monomer supports an identical pore carrying three anion-binding sites. Transient occupancy of the extracellular binding