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

Chai Ann Ng, Allan M. Torres, Guilhem Pages, Philip W. Kuchel, Jamie I. Vandenberg

    Research output: Contribution to journalArticlepeer-review

    11 Citations (Scopus)

    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.
    Original languageEnglish
    Pages (from-to)71-79
    Number of pages9
    JournalEuropean Biophysics Journal
    Volume42
    DOIs
    Publication statusPublished - 2013

    Keywords

    • NMR
    • PAS domain
    • pore domain
    • hERG

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