ArticleScientific reports2016
Structure of the Cyclic Nucleotide-Binding Homology Domain of the hERG Channel and Its Insight into Type 2 Long QT Syndrome.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 11 citations in OpenAlex.
- Integrating AI and Molecular Modeling for Structural Prediction of a Closed-Pore State of the hERG Channel.Journal of chemical information and modeling · 2026Article
- Molecular insights into the rescue mechanism of an HERG activator against severe LQT2 mutations.Journal of biomedical science · 2025Article
- Secondary Structures of the Transmembrane Domain of SARS-CoV-2 Spike Protein in Detergent Micelles.International journal of molecular sciences · 2022Article
- Mechanism of hERG inhibition by gating-modifier toxin, APETx1, deduced by functional characterization.BMC molecular and cell biology · 2021Article
- Structure of KCNH2 cyclic nucleotide-binding homology domain reveals a functionally vital salt-bridge.The Journal of general physiology · 2020Article
- L51P, a novel mutation in the PAS domain of hERG channel, confers long QT syndrome by impairing channel activation.American journal of translational research · 2020Article
- Identification of undecylenic acid as EAG channel inhibitor using surface plasmon resonance-based screen of KCNH channels.BMC pharmacology & toxicology · 2019Article
- Two mutations at different positions in the CNBH domain of the hERG channel accelerate deactivation and impair the interaction with the EAG domain.The Journal of physiology · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The human ether-à-go-go related gene (hERG) channel is crucial for the cardiac action potential by contributing to the fast delayed-rectifier potassium current. Mutations in the hERG channel result in type 2 long QT syndrome (LQT2). The hERG channel contains a cyclic nucleotide-binding homology domain (CNBHD) and this domain is required for the channel gating though molecular interactions with the eag domain. Here we present solution structure of the CNBHD of the hERG channel. The structural study reveals that the CNBHD adopts a similar fold to other KCNH channels. It is self-liganded and it contains a short β-strand that blocks the nucleotide-binding pocket in the β-roll. Folding of LQT2-related mutations in this domain was shown to be affected by point mutation. Mutations in this domain can cause protein aggregation in E. coli cells or induce conformational changes. One mutant-R752W showed obvious chemical shift perturbation compared with the wild-type, but it still binds to the eag domain. The helix region from the N-terminal cap domain of the hERG channel showed unspecific interactions with the CNBHD.
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