{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhong L"],"funding":["Macau University of Science and Technology Foundation (MUST Foundation)","National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["887-899"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12589563"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["35(11)"],"pubmed_abstract":["The KCNQ1 + KCNE1 potassium channel complex produces the slow delayed rectifier current (I<sub>Ks</sub>) critical for cardiac repolarization. Loss-of-function mutations in KCNQ1 and KCNE1 cause long QT syndrome (LQTS) types 1 and 5 (LQT1/LQT5), accounting for over one-third of clinical LQTS cases. Despite prior structural work on KCNQ1 and KCNQ1 + KCNE3, the structural basis of KCNQ1 + KCNE1 remains unresolved. Using cryo-electron microscopy and electrophysiology, we determined high-resolution (2.5-3.4 Å) structures of human KCNQ1<sub>APO</sub>, and KCNQ1 + KCNE1 in both closed and open states. KCNE1 occupies a pivotal position at the interface of three KCNQ1 subunits, inducing six helix-to-loop transitions in KCNQ1 transmembrane segments. Three of them occur at both ends of the S4-S5 link"],"journal":["Cell research"],"pubmed_title":["Secondary structure transitions and dual PIP2 binding define cardiac KCNQ1-KCNE1 channel gating."],"pmcid":["PMC12589563"],"funding_grant_id":["32171221","FRG-23-030-SKL","32271260"],"pubmed_authors":["Wan S","Peng X","Huang C","Ma L","Zhang J","Zhang H","Lin X","Nan W","Shen B","Cheng X","Zhang Q","Yu H","Yan Z","Chung SK","Wong VKW","Jiang ZH","Mou Y","Hua Y","Yang H","Neher E","Hu B","Zhou Z","Hou P","Noe F","Jiang D","Zhu W","Xiao C","Zhong L","Liu F"],"additional_accession":[]},"is_claimable":false,"name":"Secondary structure transitions and dual PIP2 binding define cardiac KCNQ1-KCNE1 channel gating.","description":"The KCNQ1 + KCNE1 potassium channel complex produces the slow delayed rectifier current (I<sub>Ks</sub>) critical for cardiac repolarization. Loss-of-function mutations in KCNQ1 and KCNE1 cause long QT syndrome (LQTS) types 1 and 5 (LQT1/LQT5), accounting for over one-third of clinical LQTS cases. Despite prior structural work on KCNQ1 and KCNQ1 + KCNE3, the structural basis of KCNQ1 + KCNE1 remains unresolved. Using cryo-electron microscopy and electrophysiology, we determined high-resolution (2.5-3.4 Å) structures of human KCNQ1<sub>APO</sub>, and KCNQ1 + KCNE1 in both closed and open states. KCNE1 occupies a pivotal position at the interface of three KCNQ1 subunits, inducing six helix-to-loop transitions in KCNQ1 transmembrane segments. Three of them occur at both ends of the S4-S5 link","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-07-15T06:33:40.471Z","creation":"2026-06-30T03:23:17.821Z"},"accession":"S-EPMC12589563","cross_references":{"pubmed":["41034624"],"doi":["10.1038/s41422-025-01182-9"]}}