Transferring knowledge towards understanding the pore stabilizing variations in K(+) channels: pore stability in K(+) channels

J Bioenerg Biomembr. 2012 Feb;44(1):199-205. doi: 10.1007/s10863-012-9407-6.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism*
  • Ion Channel Gating / genetics
  • Ion Channel Gating / physiology*
  • Models, Molecular*
  • Molecular Sequence Data
  • Mutagenesis
  • Potassium Channels, Voltage-Gated / chemistry
  • Potassium Channels, Voltage-Gated / genetics*
  • Potassium Channels, Voltage-Gated / metabolism*
  • Protein Stability*
  • Species Specificity


  • Bacterial Proteins
  • KcsA protein, Streptomyces coelicolor
  • Potassium Channels, Voltage-Gated