Conserved positioning of proline residues in membrane-spanning helices of ion-channel proteins.
Proline residues are a common feature of known and putative transmembrane helices of transport proteins. We find considerable consistency in the positioning of these residues within the structures. The proline residues are usually found on the hydrophilic (interior) faces of the pore-forming helices. This general observation adds considerable support to hypotheses concerning the structure of the ion-channels formed by alamethicin and melittin. As proline kinks helices, our observation suggests that the pores formed in ion-channel proteins tend to be funnel-shaped having a constriction near their center. Such a structure can aid in the capture of ions by the channel (an entropic effect) and should help in the gating mechanism of the channel. The observation will aid identification of putative transmembrane helices of ion-channels.
Woolfson
D N
DN
University Chemical Laboratory, Cambridge, UK.
Mortishire-Smith
R J
RJ
Williams
D H
DH
D000818:Animals; D001436:Bacteriorhodopsins / Q000737:chemistry; D002462:Cell Membrane / Q000648:ultrastructure; D004330:Drosophila; D004593:Electrophorus; D007473:Ion Channels / Q000737:chemistry*; D046911:Macromolecular Substances; D008555:Melitten / Q000737:chemistry; D008566:Membranes / Q000648:ultrastructure; D051379:Mice; D008961:Models, Structural; D011392:Proline; D011487:Protein Conformation
D007473:Ion Channels; D046911:Macromolecular Substances; D008555:Melitten; D001436:Bacteriorhodopsins; D011392:Proline