title: Peptaibols: models for ion channels.
abstract: Peptaibols are membrane-active polypeptides isolated from fungal sources. They are characterized by the presence of an unusual amino acid, alpha-aminoisobutyric acid, and a C-terminal hydroxylated amino acid. Peptaibols exhibit antibiotic activity against bacteria and fungi. Their amphipathic nature allows them to self-associate into oligomeric ion-channel assemblies which span the width of lipid bilayer membranes. Over 200 peptaibol sequences have been reported to date, which are compiled in the Peptaibol Database at http://www.cryst.bbk.ac.uk/peptaibol. Alignments of these sequences have been carried out in order to define a series of related subfamilies (SFs) with common sequence features thought to be important for channel formation. Crystal structures determined for a number of peptaibols from the various SFs provide the bases both for modelling of the channel structures and for modelling structures of other members of the same SFs.
authors.affiliation: Department of Crystallography, Birkbeck College, University of London, London WC1E 7HX, UK.
authors.forename: J K
authors.initials: JK
authors.lastname: Chugh
authors.forename: B A
authors.initials: BA
authors.lastname: Wallace
mesh_terms: D000408:Alamethicin / Q000737:chemistry; D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D007473:Ion Channels / Q000737:chemistry*; D008954:Models, Biological; D054848:Peptaibols; D010455:Peptides; D016415:Sequence Alignment
chemical_list: D000900:Anti-Bacterial Agents; D007473:Ion Channels; D054848:Peptaibols; D010455:Peptides; C116937:peptaibolin; D000408:Alamethicin