The behavior of sea anemone actinoporins at the water-membrane interface

► Actinoporins constitute a group of small and basic α-pore forming toxins produced by sea anemones. ► In water remain stably folded but upon interaction with membranes become integral membrane proteins. ► These membranes contain sphingomyelin, display phase coexistence, or both. ► Initial binding of the monomers to the membrane is accomplished by its structural β-sandwich core. ► Protein oligomerizes, N-terminal α-helix detaches, extends and builds the pore.