Channels: Sticking to nooks and crannies

Nat Chem Biol. 2013 Aug;9(8):473-4. doi: 10.1038/nchembio.1292.

Abstract

Drug design for voltage-gated ion channels has long been hampered by the absence of crystal structures and the challenge of achieving subtype selectivity. A combination of mutagenesis, electrophysiology and molecular modeling has led to the identification of a new side pocket binding site for the small molecule Psora-4 between the pore and the voltage-sensor domain of Kv1.5, offering opportunities to design allosteric ion channel modulators.

Publication types

  • News
  • Comment

MeSH terms

  • Kv1.5 Potassium Channel / antagonists & inhibitors*
  • Kv1.5 Potassium Channel / chemistry*

Substances

  • Kv1.5 Potassium Channel