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 language | English |
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Pages (from-to) | 71-79 |
Number of pages | 9 |
Journal | European Biophysics Journal |
Volume | 42 |
DOIs | |
Publication status | Published - 2013 |
Keywords
- NMR
- PAS domain
- hERG
- pore domain