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Conserved Binding Sites01:49

Conserved Binding Sites

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Mutations01:35

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Related Experiment Video

Updated: Jan 8, 2026

Functional Characterization of Endogenously Expressed Human RYR1 Variants
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Functional Characterization of Endogenously Expressed Human RYR1 Variants

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Conserved region amino acid mutations in Calcin: Altering the RyR structural-functional relationship.

Lianbo Wang1, Xiaoyu Hua2, Xiaofen Ma3

  • 1College of Veterinary Medicine, Shanxi Agricultural University, ShanXi, TaiGu, 030801, China; Faculty of Naval Medicine, Naval Medical University (Second Military Medical University), Shanghai, 200433, China.

Toxicon : Official Journal of the International Society on Toxinology
|December 22, 2025
PubMed
Summary

Charge-reversal mutations in scorpion Calcin peptides enhance Ryanodine Receptor (RyR) interaction. The E29R mutant significantly boosts calcium release, offering a basis for new peptide therapeutics targeting calcium channel diseases.

Keywords:
CalcinMolecular dockingMolecular dynamicsRyRStructural modeling

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Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
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Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Calcin peptides from scorpion venom bind Ryanodine Receptors (RyRs), modulating calcium release.
  • Previous studies indicated electrostatic interactions are key, but charge-reversal effects were unknown.

Purpose of the Study:

  • To investigate the impact of charge-reversal mutations (E12R, E12K, E29R, E29K) in OpiCa1 on its structure, RyR binding, and function.
  • To explore structure-function relationships for optimizing Calcin-based therapeutics.

Main Methods:

  • Computational modeling (molecular docking and dynamics simulations) to predict binding modes and stability.
  • Experimental validation using cellular assays to measure calcium (Ca2+) release in cardiomyocytes.

Main Results:

  • All OpiCa1 mutants retained the native inhibitor cystine knot fold but showed altered surface electrostatics.
  • Simulations predicted distinct binding interactions with RyR1 and RyR2 for each mutant.
  • The E29R mutant demonstrated significantly enhanced Ca2+ release from cardiomyocytes via RyR2 activation compared to wild-type.

Conclusions:

  • Residue E29 is critical; charge-reversal mutation to arginine (E29R) optimizes Calcin activity by improving electrostatic complementarity with RyR.
  • This provides a rational strategy for developing enhanced peptide therapeutics for calcium dysregulation diseases targeting RyRs.