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Directly acting muscle relaxants like dantrolene and botulinum toxin (BoNT) have distinct mechanisms and applications. Dantrolene, a hydantoin derivative, acts on the ryanodine receptor (RYR1) in skeletal muscle cells. RYR1 are calcium channels present at the sarcoplasmic reticulum membrane. In response to excitation, they release calcium ions from the sarcoplasmic reticulum to the cytosol. Calcium promotes actin-myosin-mediated contraction of muscles.
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Related Experiment Video

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Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
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Structural basis for diamide modulation of ryanodine receptor.

Ruifang Ma1, Omid Haji-Ghassemi2, Dan Ma1

  • 1Tianjin Key Laboratory for Modern Drug Delivery & High-Efficiency, Collaborative Innovation Center of Chemical Science and Engineering, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China.

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The highest-resolution structure of insect ryanodine receptors (RyRs) bound to chlorantraniliprole (CHL) reveals how diamide insecticides work. This discovery aids in developing new pest control agents and treatments for human muscle disorders.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Insecticide Research

Background:

  • Diamide insecticides are globally significant, targeting insect ryanodine receptors (RyRs) for pest control.
  • Understanding the molecular mechanisms of diamide action and resistance is crucial for sustainable agriculture and human health.

Purpose of the Study:

  • To determine the high-resolution cryo-electron microscopy (cryo-EM) structure of RyR1 in complex with chlorantraniliprole (CHL) in its open state.
  • To elucidate the binding site and mechanism of action of diamide insecticides.
  • To understand the molecular basis of insecticide resistance and selectivity.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to obtain the 3.2-Å structure of RyR1-CHL complex.
  • Mutagenesis studies to validate the CHL binding site and assess insecticide selectivity.
  • Analysis of structural data to identify mechanisms of insecticide resistance.

Main Results:

  • The highest-resolution cryo-EM structure of an insect RyR1 in the open state bound to chlorantraniliprole (CHL) was determined.
  • The CHL binding site was precisely mapped, revealing its interaction with the S4-S5 linker, which triggers channel opening.
  • Mutagenesis data confirmed the binding site and explained the selectivity of diamide insecticides for Lepidoptera over other species.
  • Two resistance mechanisms in pests were identified: steric hindrance and loss of contact with the insecticide.

Conclusions:

  • The detailed structure provides a mechanistic understanding of how diamide insecticides function at the molecular level.
  • This research lays the groundwork for designing novel, highly selective diamide pesticides to combat pest resistance.
  • The findings also offer insights for developing therapeutic agents targeting human RyRs for myopathies.