Insights into hERG K⁺ channel structure and function from NMR studies

Chai Ann Ng, Allan M. Torres, Guilhem Pages, Philip W. Kuchel, Jamie I. Vandenberg

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

The unique gating kinetics of hERG K⺠channels are critical for normal cardiac repolarization, and patients with mutations in hERG have a markedly increased risk of cardiac arrhythmias and sudden cardiac arrest. HERG K⺠channels are also remarkably promiscuous with respect to drug binding, which has been a very significant problem for the pharmaceutical industry. Here, we review the progress that has been made in understanding the structure and function of hERG K⺠channels with a particular focus on nuclear magnetic resonance studies of the domains of the hERG K⺠channel.
Original languageEnglish
Pages (from-to)71-79
Number of pages9
JournalEuropean Biophysics Journal
Volume42
DOIs
Publication statusPublished - 2013

Keywords

  • NMR
  • PAS domain
  • hERG
  • pore domain

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