Three-Dimensional Location of the Imperatoxin a Binding Site on the Ryanodine Receptor
Copyright policy )Three-Dimensional Location of the Imperatoxin a Binding Site on the Ryanodine Receptor
Cryo-electron microscopy and three-dimensional, single-particle image analysis have been used to reveal the specific binding site of imperatoxin A (IpTxa) on the architecture of the calcium release channel/ryanodine receptor from skeletal muscle (RyR1). IpTxa is a peptide toxin that binds with high affinity to RyR1 and affects its functioning. The toxin was derivatized with biotin to enhance its detection with streptavidin. IpTxa binds to the cytoplasmic moiety of RyR1 between the clamp and handle domains, 11 nm away from the transmembrane pore. The proposed mimicry by IpTxa of the dihydropyridine receptor (DHPR) II-III loop, thought to be a main physiological excitation-contraction trigger, suggests that the IpTxa binding location is a potential excitation-contraction signal transduction site.
- University of Wisconsin–Madison United States
- State University of New York at Potsdam United States
- University of Wisconsin–Oshkosh United States
- New York State Department of Health United States
- Wadsworth Center United States
Models, Molecular, Cytoplasm, Binding Sites, Calcium Channels, L-Type, Dose-Response Relationship, Drug, Ryanodine, Cryoelectron Microscopy, Molecular Mimicry, Biotin, Scorpion Venoms, Ryanodine Receptor Calcium Release Channel, Sarcoplasmic Reticulum, Allosteric Regulation, Animals, Calcium Channels, Rabbits, Streptavidin, Ion Channel Gating, Muscle Contraction
Models, Molecular, Cytoplasm, Binding Sites, Calcium Channels, L-Type, Dose-Response Relationship, Drug, Ryanodine, Cryoelectron Microscopy, Molecular Mimicry, Biotin, Scorpion Venoms, Ryanodine Receptor Calcium Release Channel, Sarcoplasmic Reticulum, Allosteric Regulation, Animals, Calcium Channels, Rabbits, Streptavidin, Ion Channel Gating, Muscle Contraction
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