Oligomerization and hemolytic properties of the C-terminal domain of pyolysin, a cholesterol-dependent cytolysin.

@article{Pokrajac2013OligomerizationAH,
  title={Oligomerization and hemolytic properties of the C-terminal domain of pyolysin, a cholesterol-dependent cytolysin.},
  author={Lisa Pokrajac and J. Robin Harris and Naghmeh S. Sarraf and Michael Palmer},
  journal={Biochemistry and cell biology = Biochimie et biologie cellulaire},
  year={2013},
  volume={91 2},
  pages={59-66}
}
Pyolysin (PLO) belongs to the homologous family of the cholesterol-dependent cytolysins (CDCs), which bind to cell membranes containing cholesterol to form oligomeric pores of large size. The CDC monomer structure consists of 4 domains. Among these, the C-terminal domain 4 has been implicated in membrane binding of the monomer, while the subsequent processes of oligomerization and membrane insertion have primarily been assigned to other domains of the molecule. Recombinantly expressed or… CONTINUE READING

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