Primary and secondary structure of the pore-forming peptide of pathogenic Entamoeba histolytica.

@article{Leippe1992PrimaryAS,
  title={Primary and secondary structure of the pore-forming peptide of pathogenic Entamoeba histolytica.},
  author={Matthias Leippe and Egbert Tannich and Rainer Nickel and Gisou F van der Goot and Franc Pattus and R Horstmann and HANS J. MUELLER-EBERHARD},
  journal={The EMBO journal},
  year={1992},
  volume={11 10},
  pages={3501-6}
}
A pore-forming peptide is implicated in the potent cytolytic activity of pathogenic Entamoeba histolytica. Using NH2-terminal sequence information of this peptide, the corresponding cDNA was isolated. The cDNA-deduced amino acid sequence revealed a putative signal peptide and a mature peptide of 77 amino acids including six cysteine residues. Computer-aided secondary structure analysis predicted that the peptide would be composed of four adjacent alpha-helices, and CD spectroscopy indicated an… CONTINUE READING

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