This high affinity to the ‘Shaker K’ channel is dependent on the residues of Arg 24, Lys 27, and Arg 31.[1] The ability of the agitoxin to block the ‘Shaker K’ channel suggests a docking mechanism whereby the toxin sits on the channel and then prevents its opening through flexible movements of the side chains thereby allowing for various protein-protein complexes to be enacted.[3] AgTx2 has been found to undergo conformational changes when bound to the ‘Shaker K’ channel which suggests the induced fit model may be present in toxin-channel interaction.