Structural Basis for the Modulation of Ryanodine Receptors.

Deshun Gong, Nieng Yan, Hannah A Ledford

Trends in biochemical sciences 2021 Jun

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Historically, ryanodine receptors (RyRs) have presented unique challenges for high-resolution structural determination despite long-standing interest in their role in excitation-contraction coupling. Owing to their large size (nearly 2.2 MDa), high-resolution structures remained elusive until the advent of cryogenic electron microscopy (cryo-EM) techniques. In recent years, structures for both RyR1 and RyR2 have been solved at near-atomic resolution. Furthermore, recent reports have delved into their more complex structural associations with key modulators - proteins such as the dihydropyridine receptor (DHPR), FKBP12/12.6, and calmodulin (CaM), as well as ions and small molecules including Ca2+, ATP, caffeine, and PCB95. This review addresses the modulation of RyR1 and RyR2, in addition to the impact of such discoveries on intracellular Ca2+ dynamics and biophysical properties. Copyright © 2020 Elsevier Ltd. All rights reserved.

Citation

Deshun Gong, Nieng Yan, Hannah A Ledford. Structural Basis for the Modulation of Ryanodine Receptors. Trends in biochemical sciences. 2021 Jun;46(6):489-501