title: Cryptic clues as to how water-soluble protein toxins form pores in membranes.
abstract: Pore-forming protein toxins possess the remarkable property that they can exist either in a stable water-soluble state or as an integral membrane pore. In order to convert from the water-soluble to the membrane state, the toxin must undergo large conformational changes. Recent work on a class of pore-forming toxins that are rich in beta-sheet content suggests a common mechanism of membrane insertion may exist despite these toxins possessing very different primary, tertiary and quaternary structures.
authors.affiliation: Biota Structural Biology Laboratory, St Vincent's Institute of Medical Research, 9 Princes Street, Fitzroy, Victoria 3065, Australia. mwp@rubens.its.unimelb.edu.au
authors.forename: Michael W
authors.initials: MW
authors.lastname: Parker
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000494:pharmacology*; D001427:Bacterial Toxins / Q000737:chemistry / Q000494:pharmacology*; D002462:Cell Membrane / Q000737:chemistry / Q000187:drug effects* / Q000502:physiology; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D011487:Protein Conformation; D020539:Sequence Analysis, Protein
chemical_list: D001426:Bacterial Proteins; D001427:Bacterial Toxins