Leucine zipper
A leucine zipper (or leucine scissors) is a common three-dimensional structural motif in proteins. It was first described by Landschulz and collaborators in 1988 when they found that an enhancer binding protein had a very characteristic 30-amino acid segment, and the display of these amino acid sequences on an idealized alpha helix revealed a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns.