ArticlePLoS computational biology2009
A structural model of the pore-forming region of the skeletal muscle ryanodine receptor (RyR1).
Article in PLoS computational biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Correlation of phenotype with genotype and protein structure in RYR1-related disorders.Journal of neurology · 2018Trial
- Resveratrol Directly Controls the Activity of Neuronal Ryanodine Receptors at the Single-Channel Level.Molecular neurobiology · 2020Article
- Interaction of ions with the luminal sides of wild-type and mutated skeletal muscle ryanodine receptors.Journal of molecular modeling · 2016Article
- FRET-based trilateration of probes bound within functional ryanodine receptors.Biophysical journal · 2014Article
- Pore dynamics and conductance of RyR1 transmembrane domain.Biophysical journal · 2014Article
- Investigations of the contribution of a putative glycine hinge to ryanodine receptor channel gating.The Journal of biological chemistry · 2013Article
- Ca2+ release in muscle fibers expressing R4892W and G4896V type 1 ryanodine receptor disease mutants.PloS one · 2013Article
- Article
- Identification of functionally critical residues in the channel domain of inositol trisphosphate receptors.The Journal of biological chemistry · 2012Article
- Protein kinase A (PKA) phosphorylation of Na+/K+-ATPase opens intracellular C-terminal water pathway leading to third Na+-binding site in molecular dynamics simulations.The Journal of biological chemistry · 2012Article
- Type 1 ryanodine receptor knock-in mutation causing central core disease of skeletal muscle also displays a neuronal phenotype.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Article
- Three-dimensional structure of recombinant type 1 inositol 1,4,5-trisphosphate receptor.The Biochemical journal · 2010Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Ryanodine receptors (RyRs) are ion channels that regulate muscle contraction by releasing calcium ions from intracellular stores into the cytoplasm. Mutations in skeletal muscle RyR (RyR1) give rise to congenital diseases such as central core disease. The absence of high-resolution structures of RyR1 has limited our understanding of channel function and disease mechanisms at the molecular level. Here, we report a structural model of the pore-forming region of RyR1. Molecular dynamics simulations show high ion binding to putative pore residues D4899, E4900, D4938, and D4945, which are experimentally known to be critical for channel conductance and selectivity. We also observe preferential localization of Ca(2+) over K(+) in the selectivity filter of RyR1. Simulations of RyR1-D4899Q mutant show a loss of preference to Ca(2+) in the selectivity filter as seen experimentally. Electrophysiological experiments on a central core disease mutant, RyR1-G4898R, show constitutively open channels that conduct K(+) but not Ca(2+). Our simulations with G4898R likewise show a decrease in the preference of Ca(2+) over K(+) in the selectivity filter. Together, the computational and experimental results shed light on ion conductance and selectivity of RyR1 at an atomistic level.
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