Characterization of the Lipid-Binding Site of Equinatoxin II by NMR and Molecular Dynamics Simulation.

@article{Weber2015CharacterizationOT,
  title={Characterization of the Lipid-Binding Site of Equinatoxin II by NMR and Molecular Dynamics Simulation.},
  author={Daniel K. Weber and Shenggen Yao and Nejc Rojko and Gregor Anderluh and Terry P. Lybrand and Matthew T. Downton and John E Wagner and Frances Separovic},
  journal={Biophysical journal},
  year={2015},
  volume={108 8},
  pages={1987-96}
}
Equinatoxin II (EqtII) is a soluble, 20 kDa pore-forming protein toxin isolated from the sea anemone Actinia equina. Although pore formation has long been known to occur in distinct stages, including monomeric attachment to phospholipid membranes followed by detachment of the N-terminal helical domain and oligomerization into the final pore assembly, atomistic-level detail of the protein-lipid interactions underlying these events remains elusive. Using high-resolution solution state NMR of… CONTINUE READING