Evidence that clustered phosphocholine head groups serve as sites for binding and assembly of an oligomeric protein pore.

@article{Valeva2006EvidenceTC,
  title={Evidence that clustered phosphocholine head groups serve as sites for binding and assembly of an oligomeric protein pore.},
  author={Angela Valeva and Nadja Hellmann and Iwan Walev and Donn Allan Strand and Markus Plate and Fatima Boukhallouk and Antje Brack and Kentaro Hanada and Heinz Decker and Sucharit Bhakdi},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 36},
  pages={
          26014-21
        }
}
High susceptibility of rabbit erythrocytes toward the pore-forming action of staphylococcal alpha-toxin correlates with the presence of saturable, high affinity binding sites. All efforts to identify a protein or glycolipid receptor have failed, and the fact that liposomes composed solely of phosphatidylcholine are efficiently permeabilized adds to the enigma. A novel concept is advanced here to explain the puzzle. We propose that low affinity binding moieties can assume the role of high… CONTINUE READING
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