Common structural features in gramicidin and other ion channels.
This review compares and contrasts the structures of several different types of ion channels with known three-dimensional structures, including gramicidin and the family of peptaibol channels, as well as the Streptomyces lividans potassium channel, to reveal common features in their structures that relate to their functional roles in ion binding and transport across membranes. Specifically, the locations of aromatic amino acids, the dimensions of the molecules, the multimeric nature of the channels and the roles of hydrogen bonds in stabilising such structures, the means by which the channels open and close, and the chemical nature of the groups which make up the channel lumen are discussed. The emphasis is on the commonality of features found in model channels, which may ultimately be found in other biological channel structures.
Wallace
B A
BA
Department of Crystallography, Birkbeck College, University of London, London WC1E 7HX, UK. ubcg91c@ccs.bbk.ac.uk
D000595:Amino Acid Sequence; D006096:Gramicidin / Q000737:chemistry*; D007473:Ion Channels / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015221:Potassium Channels / Q000737:chemistry; D011487:Protein Conformation; D013302:Streptomyces / Q000502:physiology
D007473:Ion Channels; D015221:Potassium Channels; D006096:Gramicidin