biostudies-literatureButler ABritish Heart Foundation1572https://www.ebi.ac.uk/biostudies/studies/S-EPMC6992539biostudies-literatureUnknown10The human voltage-sensitive K⁺ channel hERG plays a fundamental role in cardiac action potential repolarization, effectively controlling the QT interval of the electrocardiogram. Inherited loss- or gain-of-function mutations in hERG can result in dangerous "long" (LQTS) or "short" QT syndromes (SQTS), respectively, and the anomalous susceptibility of hERG to block by a diverse range of drugs underlies an acquired LQTS. A recent open channel cryo-EM structure of hERG should greatly advance understanding of the molecular basis of hERG channelopathies and drug-induced LQTS. Here we describe an update of recent research that addresses the nature of the particular gated state of hERG captured in the new structure, and the insight afforded by the structure into the molecular basis forFrontiers in pharmacologyAn Update on the Structure of hERG.PMC6992539PG/17/89/33414FS/14/38/30868Dempsey CEButler AHancox JCHelliwell MVZhang YfalseAn Update on the Structure of hERG.The human voltage-sensitive K⁺ channel hERG plays a fundamental role in cardiac action potential repolarization, effectively controlling the QT interval of the electrocardiogram. Inherited loss- or gain-of-function mutations in hERG can result in dangerous "long" (LQTS) or "short" QT syndromes (SQTS), respectively, and the anomalous susceptibility of hERG to block by a diverse range of drugs underlies an acquired LQTS. A recent open channel cryo-EM structure of hERG should greatly advance understanding of the molecular basis of hERG channelopathies and drug-induced LQTS. Here we describe an update of recent research that addresses the nature of the particular gated state of hERG captured in the new structure, and the insight afforded by the structure into the molecular basis for2019-01-01T00:00:00Z20192025-04-25T21:12:39.665Z2020-05-22T10:23:45ZS-EPMC69925393203824810.3389/fphar.2019.01572