title: Cytolytic pore-forming proteins and peptides: is there a common structural motif?
abstract: Pore-forming proteins or peptides (PFP) have now been isolated from a wide array of species ranging from humans to bacteria. A great number of these toxins lyse cells through a 'barrel-stave' mechanism, in which monomers of the toxin bind to and insert into the target membrane and then aggregate like barrel staves surrounding a central, water-filled pore. An evaluation of the secondary structures suggest that common secondary structures may be employed by most of these toxic PFP.
authors.affiliation: Laboratory of Cellular Physiology and Immunology, Rockfeller University, New York, NY 10021.
authors.forename: D M
authors.initials: DM
authors.lastname: Ojcius
authors.forename: J D
authors.initials: JD
authors.lastname: Young
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D018272:Porins; D011487:Protein Conformation
chemical_list: D001425:Bacterial Outer Membrane Proteins; D010455:Peptides; D018272:Porins