Structural basis for tetrodotoxin-resistant sodium channel binding by μ-conotoxin SmIIIA

SmIIIA is a new μ-conotoxin isolated recently from Conus stercusmuscarum. Although it shares several biochemical characteristics with other μ-conotoxins (the arrangement of cysteine residues and a conserved arginine believed to interact with residues near the channel pore), it has several distinctive features, including the absence of hydroxyproline, and is the first specific antagonist of tetrodotoxin-resistant voltage-gated sodium channels to be characterized.