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- W4284896612 abstract "In this issue of Structure, Melville and colleagues used cryo-EM to study the binding of ryanodine receptors to Rycals, compounds with the potential to treat skeletal and cardiac muscle disorders. Unexpectedly, they found that Rycal packs against an ATP in a peripheral pocket, which stabilizes the closed channel state. In this issue of Structure, Melville and colleagues used cryo-EM to study the binding of ryanodine receptors to Rycals, compounds with the potential to treat skeletal and cardiac muscle disorders. Unexpectedly, they found that Rycal packs against an ATP in a peripheral pocket, which stabilizes the closed channel state. A drug and ATP binding site in type 1 ryanodine receptorMelville et al.StructureMay 16, 2022In BriefMelville et al. show the cryo-EM structure of the ARM210-bound ryanodine receptor. The Rycal compound (ARM210) binds cooperatively with ATP in a second ATP-binding site and stabilizes the closed state of the channel. This site may be a metabolic sensor as it binds two ADP but only one ATP. Full-Text PDF" @default.
- W4284896612 created "2022-07-09" @default.
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- W4284896612 date "2022-07-01" @default.
- W4284896612 modified "2023-09-30" @default.
- W4284896612 title "It takes two to tango: Rycals and ATP snuggle up to bind ryanodine receptors" @default.
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- W4284896612 doi "https://doi.org/10.1016/j.str.2022.05.022" @default.
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