Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process.

@article{Unno2014HemolyticLC,
  title={Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process.},
  author={Hideaki Unno and Shuichiro Goda and Tomomitsu Hatakeyama},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 18},
  pages={12805-12}
}
CEL-III is a hemolytic lectin isolated from the sea cucumber Cucumaria echinata. This lectin is composed of two carbohydrate-binding domains (domains 1 and 2) and one oligomerization domain (domain 3). After binding to the cell surface carbohydrate chains through domains 1 and 2, domain 3 self-associates to form transmembrane pores, leading to cell lysis or death, which resembles other pore-forming toxins of diverse organisms. To elucidate the pore formation mechanism of CEL-III, the crystal… CONTINUE READING

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Crystal structure of the pore-forming CEL-III heptamer

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