This domain is approximately 150 amino acids in length and is always found located at the N-termini of proteins.

The domain forms a compact globular structure, composed of nine alpha-helices connected by loops of varying length.

Epsin binding to membranes facilitates their deformation by insertion of the N-terminal helix into the inner leaflet of the bilayer, pushing the head groups apart.

This points to a pioneering role for epsin in vesicle budding, as it provides both a driving force and a link between membrane invagination and clathrin polymerisation.

Binding causes tubulation of liposomes and in vivo this membrane-binding function is normally coordinated with clathrin polymerisation.