Ontology highlight
ABSTRACT:
SUBMITTER: Leippe M
PROVIDER: S-EPMC556807 | biostudies-other | 1992 Oct
REPOSITORIES: biostudies-other
Leippe M M Tannich E E Nickel R R van der Goot G G Pattus F F Horstmann R D RD Müller-Eberhard H J HJ
The EMBO journal 19921001 10
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 a ...[more]