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The sodium channel α subunit comprises four domains, each containing six transmembrane segments, with the 5th and 6th segments responsible for pore formation. The β subunits consist of a single membrane-spanning segment and feature an immunoglobulin-like fold in their extracellular domain. Notably, the α subunit includes multiple binding sites for various toxins and drugs, demonstrating its crucial role in the channel's functionality and interaction with pharmacological agents.
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Sodium Channel Structure The a subunit consists of four domains of six transmembrane segments, with the 5th and 6th segments comprising the pore formation unit. The b subunits consist of a single membrane spanning segment with an immunoglobulin-like fold in an extracellular domain. The a subunit contains the binding sites for a variety of toxins and drugs, as indicated.