ArticleBiophysical journal2008
Structural and functional characterization of ryanodine receptor-natrin toxin interaction.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 50 citations in OpenAlex.
- Venom Proteins of the FireflyToxins · 2025Article
- Article
- Snake Venom Components as Therapeutic Drugs in Ischemic Heart Disease.Biomolecules · 2023Review
- Genomic Structure of Two Kv1.3 Channel Blockers from Scorpion Mesobuthus eupeus and Sea Anemone Stichodactyla haddoni and Construction of their Chimeric Peptide as a Novel Blocker.Biochemical genetics · 2022Article
- An Emergent Role for Mitochondrial Bioenergetics in the Action of Snake Venom Toxins on Cancer Cells.Frontiers in oncology · 2022Review
- CRISPs Function to Boost Sperm Power Output and Motility.Frontiers in cell and developmental biology · 2021Article
- Proteomic Investigations of Two PakistaniToxins · 2020Article
- Review
- Crystal structure of the complex between venom toxin and serum inhibitor from Viperidae snake.The Journal of biological chemistry · 2019Article
- CRISP1 as a novel CatSper regulator that modulates sperm motility and orientation during fertilization.The Journal of cell biology · 2015Article
- Impaired local regulation of ryanodine receptor type 2 by protein phosphatase 1 promotes atrial fibrillation.Cardiovascular research · 2014Article
- Eukaryotic expression, purification and structure/function analysis of native, recombinant CRISP3 from human and mouse.Scientific reports · 2014Article
- Structure of glutaraldehyde cross-linked ryanodine receptor.Journal of structural biology · 2013Article
- Ligand-dependent conformational changes in the clamp region of the cardiac ryanodine receptor.The Journal of biological chemistry · 2013Article
- Modeling a ryanodine receptor N-terminal domain connecting the central vestibule and the corner clamp region.The Journal of biological chemistry · 2013Article
- The role of cysteine-rich secretory proteins in male fertility.Asian journal of andrology · 2011Review
- Cobra CRISP functions as an inflammatory modulator via a novel Zn2+- and heparan sulfate-dependent transcriptional regulation of endothelial cell adhesion molecules.The Journal of biological chemistry · 2010Article
- Dynamic, inter-subunit interactions between the N-terminal and central mutation regions of cardiac ryanodine receptor.Journal of cell science · 2010Article
- CLIC2-RyR1 interaction and structural characterization by cryo-electron microscopy.Journal of molecular biology · 2009Article
- Article
Corrections and comments
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Authors and funding
9 authors at 6 institutions in 2 countries.
Funding
Abstract
Cysteine-rich secretory proteins (CRISPs) are widely distributed, and notably occur in the mammalian reproductive tract and in the salivary glands of venomous reptiles. Most CRISPs can inhibit ion channels, such as the cyclic nucleotide-gated ion channel, potassium channel, and calcium channel. Natrin is a CRISP that has been purified from snake venom. Its targets include the calcium-activated potassium channel, the voltage-gated potassium channel, and the calcium release channel/ryanodine receptor (RyR). Immunoprecipitation experiments showed that natrin binds specifically to type 1 RyR (RyR1) from skeletal muscle. Natrin was found to inhibit both the binding of ryanodine to RyR1, and the calcium-channel activity of RyR1. Cryo-electron microscopy and single-particle image reconstruction analysis revealed that natrin binds to the clamp domains of RyR1. Docking of the crystal structure of natrin into our cryo-electron microscopy density map of the RyR1 + natrin complex suggests that natrin inhibits RyR1 by stabilizing a domain-domain interaction, and that the cysteine-rich domain of natrin is crucial for binding. These findings help reveal how natrin toxin inhibits the RyR calcium release channel, and they allow us to posit a generalized mechanism that governs the interaction between CRISPs and ion channels.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.