Open-state structure and pore gating mechanism of the cardiac sodium channel

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Open-state structure and pore gating mechanism of the cardiac sodium channelUsing a mutation to block fast sodium channel inactivation, the open-state structure of the primary cardiac sodium channel NaV1.5 was captured, revealing the molecular mechanisms for rapid opening and fast inactivation of the pore as well as the receptor site for high-affinity binding of the open-state sodium channel blocker propafenone.Using a mutation to block fast sodium channel inactivation, the open-state structure of the primary cardiac sodium channel NaV1.5 was captured, revealing the molecular mechanisms for rapid opening and fast inactivation of the pore as well as the receptor site for high-affinity binding of the open-state sodium channel blocker propafenone.Daohua Jiang, Richard Banh, Tamer M. Gamal El-Din, Lige Tonggu, Michael J. Lenaeus, Régis Pomès, Ning Zheng, William A. Catterallhttps://secure.jbs.elsevierhealth.com/action/getSharedSiteSession?redirect=https%3A%2F%2Fwww.cell.com%2Fcell%2Ffulltext%2FS0092-8674%2821%2900995-8%3Frss%3Dyes&rc=0http://www.cell.com/cell/inpress.rssCellCell RSS feed.Wireless News CampaignSeptember 14, 2021

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