K(+) channels are macromolecules embedded in biological membranes, where they play a key role in cellular excitability and signal transduction pathways. Knowledge of their structure should help improve our understanding of their function and lead to the design of therapeutic compounds. Most pharmacological and structural characteristics of these channels have been elucidated by using high-affinity channel blockers isolated from scorpion venoms. Recent data on the three-dimensional structures of K(+) channels and novel scorpion toxins suggest a variety of novel interacting modes of these channels and toxins, which should help increase our understanding of the K(+) channel structure-function relationship.