The structure of the neurotoxin palytoxin determined by MicroED
Abstract
Palytoxin (PTX) is a potent neurotoxin found in marine animals that can cause serious symptoms such as muscle contractions, haemolysis of red blood cells and potassium leakage. Despite years of research, very little is known about the mechanism of PTX. However, recent advances in the field of cryoEM, specifically the use of microcrystal electron diffraction (MicroED), have allowed us to determine the structure of PTX. It was discovered that PTX folds into a hairpin motif and is able to bind to the extracellular gate of Na,K-ATPase, which is responsible for maintaining the electrochemical gradient across the plasma membrane. These findings, along with molecular docking simulations, have provided important insights into the mechanism of PTX and can potentially aid in the development of molecular agents for treating cases of PTX exposure.
02 /Specification & Classification
Click any tag to browse matching papers- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Characterisation of palytoxin from an undescribed Palythoa (Anthozoa: Zoantharia: Sphenopidae) with significant in vitro cytotoxic effects on cancer cells at picomolar doses
Ludovic Sawelew, Frédéric Gault, … Jean Lorquin·bioRxiv·Mar 30, 2018
- Membrane insertion of α-xenorhabdolysin in near-atomic detail
Evelyn Schubert, Ingrid R. Vetter, … Stefan Raunser·eLifePeer-reviewed·Jul 16, 2018
- Molecular architecture of black widow spider neurotoxins
M. Chen, D. Blum, … C. Gatsogiannis·bioRxiv·Apr 19, 2021
- Molecular mechanism of α-latrotoxin action
Björn Udo Klink, Azadeh Alavizargar, … Christos Gatsogiannis·Nature CommunicationsPeer-reviewed·Oct 3, 2024
- Atomic structure and plasticity of the MthK-CTX complex investigated by cryo-EM, NMR, and MD simulations
Denis Qoraj, Swantje Mohr, … Adam Lange·Nature CommunicationsPeer-reviewed·Aug 20, 2026
- Saxiphilin is a broad-spectrum toxin sponge for C13-modified saxitoxins
Sandra Zakrzewska, Zhou Chen, … Daniel L. Minor·StructurePeer-reviewed·Jun 17, 2026