Recently, researchers from the University of Washington and other scientific research institutions published an article entitled "Structure of the Cardiac Sodium Channel" on Cell, which analyzed the structure of cardiac sodium channels. This study provides a detailed analysis of Na v1.5 structure, pharmacology, activation, inactivation, ion selectivity, and arrhythmia. (Excerpt from Cell, Published: 19 December 2019) Friction And Wear Testing Machine
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The voltage-gated sodium channel Na v1.5 generates a heart action potential and initiates a heartbeat. In this study, researchers analyzed the structure of Na v1.5 at a resolution of 3.2-3.5 ?. Na v1.5 differs from other sodium channels in that the unique sugar moiety and the Na vβ subunit interaction site lose their ability to bind disulfide bonds. The antiarrhythmic drug flecainide specifically targets the central cavity of the hole. The voltage sensor is partially activated and the quick deactivation door is partially closed. The activation of the domain III voltage sensor allows the isoleucine-phenylalanine-methionine (IFM) motif to bind to the inactivation gate receptor.
Aspartic acid and alanine are arranged on the wall of the ion selective filter, while glutamic acid and lysine are in a position to receive and release Na + ions through the charge delocalization network. Arrhythmogenic mutation sites undergo a large translocation during gating, thus providing a potential mechanism for pathogenic effects. 