Alpha toxins bind voltage-independently at site-3 of sodium channels and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin acts on Nav1.2/SCN2A. Also binds to Cav3.1/CACNA1G and Cav3.2/CACNA1H T-type calcium channels with high affinity and inhibits the channels by modifying voltage-dependent gating. Another study (PubMed:11896142) shows that it also targets neuronal high-threshold calcium channels, including P-type, N-type, and L-type calcium channels (Cav), and others that still are unidentified pharmacologically. Expressed by the venom gland. Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta). This toxin does not affect Cav1.2/CACNA1C, Cav2.1/CACNA1A, Cav2.2/CACNA1B, and Cav2.3/CACNA1E calcium channels. Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily.