title: Transferring knowledge towards understanding the pore stabilizing variations in K(+) channels: pore stability in K(+) channels.
abstract: Recent advances in structural biology underlying mechanisms of channel gating have strengthened our knowledge about how K(+) channels can be inter-convertible between conductive and non-conductive states. We have reviewed and combined mutagenesis with biochemical, biophysical and structural information in order to understand the critical roles of the pore residues in stabilizing the pore structure and channel open state. We also discuss how the latest knowledge on the K(+) channel KcsA may provide a step towards better understanding of distinct pore stabilizing differences among diversified K(+) channels.
authors.affiliation: School of Molecular and Systems Medicine, Alberta Diabetes Institute, University of Alberta, 6126 HRIF East, Edmonton AB T6G 2E1, Canada. mraja@pmcol.ualberta.ca
authors.forename: Mobeen
authors.initials: M
authors.lastname: Raja
authors.forename: Nick K
authors.initials: NK
authors.lastname: Olrichs
authors.forename: Elisabeth
authors.initials: E
authors.lastname: Vales
authors.forename: Hildgund
authors.initials: H
authors.lastname: Schrempf
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D015640:Ion Channel Gating / Q000235:genetics / Q000502:physiology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016296:Mutagenesis; D024642:Potassium Channels, Voltage-Gated / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D055550:Protein Stability; D013045:Species Specificity
chemical_list: D001426:Bacterial Proteins; C504448:KcsA protein, Streptomyces coelicolor; D024642:Potassium Channels, Voltage-Gated