Key result
Mutations designed in the linker and pore-lining helices of the ryanodine receptor type 1 (RyR1) altered channel open probability, demonstrating that the interface between these helices controls channel gating.
Population
Skeletal muscle Ryanodine receptor type 1 (RyR1) models and single channel experiments
Comparison
Mutations in the linker helix and pore-lining… vs Wild-type (WT) RyR1
Design
Preclinical
Authors
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No immediate clinical implications for RyR1 disorders; leaves open targeted modulation of this gating interface in future studies.
Identification of an interface between the pore-lining helix and a linker helix that controls RyR1 gating provides structural insights into the function of this large ion channel.
Ramachandran et al. (2013) studied this question. Site-directed mutagenesis of RyR1 (S4-S5 linker and S6 helices) vs. Wild-type RyR1 was evaluated on Channel open probability (Po) and gating characteristics. Mutations designed in the linker and pore-lining helices of the ryanodine receptor type 1 (RyR1) altered channel open probability, demonstrating that the interface between these helices controls channel gating.
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