Structural Basis for the Modulation of Ryanodine Receptors

Deshun Gong, Nieng Yan, Hannah A. Ledford

Research output: Contribution to journalReview articlepeer-review

8 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)489-501
Number of pages13
JournalTrends in Biochemical Sciences
Issue number6
StatePublished - Jun 2021

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Biochemistry


  • Ca channel
  • RyR1
  • RyR2
  • allosteric regulation
  • cryo-EM
  • excitation–contraction coupling


Dive into the research topics of 'Structural Basis for the Modulation of Ryanodine Receptors'. Together they form a unique fingerprint.

Cite this