Pore size matters for potassium channel conductance

J Gen Physiol. 2016 Oct;148(4):277-91. doi: 10.1085/jgp.201611625. Epub 2016 Sep 12.

Abstract

Ion channels are membrane proteins that mediate efficient ion transport across the hydrophobic core of cell membranes, an unlikely process in their absence. K(+) channels discriminate K(+) over cations with similar radii with extraordinary selectivity and display a wide diversity of ion transport rates, covering differences of two orders of magnitude in unitary conductance. The pore domains of large- and small-conductance K(+) channels share a general architectural design comprising a conserved narrow selectivity filter, which forms intimate interactions with permeant ions, flanked by two wider vestibules toward the internal and external openings. In large-conductance K(+) channels, the inner vestibule is wide, whereas in small-conductance channels it is narrow. Here we raise the idea that the physical dimensions of the hydrophobic internal vestibule limit ion transport in K(+) channels, accounting for their diversity in unitary conductance.

Publication types

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

MeSH terms

  • Ion Transport / physiology
  • Models, Molecular
  • Potassium / metabolism*
  • Potassium Channels / chemistry*
  • Potassium Channels / metabolism*
  • Protein Conformation

Substances

  • Potassium Channels
  • Potassium

Associated data

  • GENBANK/AAA61276
  • GENBANK/AAC31761
  • GENBANK/AAX11186
  • RefSeq/NP_000208
  • RefSeq/NP_001240307
  • RefSeq/NP_002224
  • RefSeq/NP_002226
  • RefSeq/NP_004761
  • RefSeq/NP_004965
  • RefSeq/NP_005540
  • RefSeq/NP_728123
  • SWISSPROT/O27564
  • SWISSPROT/P0A334
  • SWISSPROT/Q9YDF8
  • PDB/1K4C
  • PDB/1ORQ
  • PDB/2R9R
  • PDB/4HYO