Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin

@article{Ramachandran2002StructuralII,
  title={Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin},
  author={Rajesh Ramachandran and Alejandro P Heuck and Rodney K. Tweten and Arthur E. Johnson},
  journal={Nature Structural Biology},
  year={2002},
  volume={9},
  pages={823-827}
}
Perfringolysin O (PFO), a cytolytic toxin secreted by pathogenic Clostridium perfringens, forms large pores in cholesterol-containing membranes. Domain 4 (D4) of the protein interacts first with the membrane and is responsible for cholesterol recognition. By using several independent fluorescence techniques, we have determined the topography of D4 in the membrane-inserted oligomeric form of the toxin. Only the short hydrophobic loops at the tip of the D4 β-sandwich are exposed to the bilayer… CONTINUE READING

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