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

European Biophysics Journal : EBJ
Chai Ann NgJamie I Vandenberg

Abstract

The unique gating kinetics of hERG K(+) 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(+) 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(+) channels with a particular focus on nuclear magnetic resonance studies of the domains of the hERG K(+) channel.

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Citations

Mar 19, 2014·Journal of Structural Biology·Qingxin LiCongbao Kang
Oct 22, 2014·Journal of Peptide Science : an Official Publication of the European Peptide Society·Qingxin LiCongBao Kang
Jul 26, 2017·Clinical and Experimental Pharmacology & Physiology·JianHua HuoAiqun Ma
Sep 4, 2019·PloS One·Bryan CernudaZafir Buraei

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