Abstract
Ion Channels Voltage-gated sodium (Nav) channels have been implicated in cardiac and neurological disorders. There are many subtypes of these channels, making it challenging to develop specific therapeutics. A core α subunit is sufficient for voltage sensing and ion conductance, but function is modulated by β subunits and by natural toxins that can either act as pore blockers or gating modifiers (see the Perspective by Chowdhury and Chanda). Shen et al. present the structures of Nav1.7 in complex with both β1 and β2 subunits and with animal toxins. Pan et al. present the structure of Nav1.2 bound to β2 and a toxic peptide, the µ-conotoxin KIIIA. The structure shows why KIIIA is specific for Nav1.2. These and other recently determined Nav structures provide a framework for targeted drug development. Science , this issue p. [1303][1], p. [1309][2]; see also p. [1278][3] [1]: /lookup/doi/10.1126/science.aaw2493 [2]: /lookup/doi/10.1126/science.aaw2999 [3]: /lookup/doi/10.1126/science.aaw8645
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