The open pore conformation of potassium channels

Nature. 2002 May 30;417(6888):523-6. doi: 10.1038/417523a.


Living cells regulate the activity of their ion channels through a process known as gating. To open the pore, protein conformational changes must occur within a channel's membrane-spanning ion pathway. KcsA and MthK, closed and opened K(+) channels, respectively, reveal how such gating transitions occur. Pore-lining 'inner' helices contain a 'gating hinge' that bends by approximately 30 degrees. In a straight conformation four inner helices form a bundle, closing the pore near its intracellular surface. In a bent configuration the inner helices splay open creating a wide (12 A) entryway. Amino-acid sequence conservation suggests a common structural basis for gating in a wide range of K(+) channels, both ligand- and voltage-gated. The open conformation favours high conduction by compressing the membrane field to the selectivity filter, and also permits large organic cations and inactivation peptides to enter the pore from the intracellular solution.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Electric Conductivity
  • Ion Channel Gating*
  • Ligands
  • Membrane Potentials
  • Methanobacterium / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Potassium Channels / chemistry*
  • Potassium Channels / metabolism*
  • Potassium Channels, Calcium-Activated / chemistry
  • Potassium Channels, Calcium-Activated / metabolism
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Subunits
  • Sequence Alignment
  • Static Electricity
  • Structure-Activity Relationship


  • Bacterial Proteins
  • Ligands
  • Potassium Channels
  • Potassium Channels, Calcium-Activated
  • Protein Subunits
  • prokaryotic potassium channel

Associated data

  • PDB/1LNQ