title: Insights into hERG K+ channel structure and function from NMR studies.
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.
authors.affiliation: Mark Cowley Lidwill Research Programme in Cardiac Electrophysiology, Molecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, 405 Liverpool Street, Darlinghurst, NSW, 2010, Australia. a.ng@victorchang.edu.au
authors.forename: Chai Ann
authors.initials: CA
authors.lastname: Ng
authors.forename: Allan M
authors.initials: AM
authors.lastname: Torres
authors.forename: Guilhem
authors.initials: G
authors.lastname: Pagès
authors.forename: Philip W
authors.initials: PW
authors.lastname: Kuchel
authors.forename: Jamie I
authors.initials: JI
authors.lastname: Vandenberg
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D051638:Ether-A-Go-Go Potassium Channels / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D062105:Molecular Docking Simulation; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary
chemical_list: D051638:Ether-A-Go-Go Potassium Channels; C496884:KCNH1 protein, human