Leucine Zipper (leucine zipper): A structural primitive (motif) in the presence of DNA binding proteins and other proteins. A leucine zipper is formed when the hydrophobic surface (often containing leucine residues) of two dual-use α-spirals from the same or different polypeptide chains interacts to form a two-body structure of the loop.
Leucine Zipper (leucine zipper) is made up of stretched amino acids, each of the 7 amino acids in the 7th amino acid is leucine, leucine is hydrophobic amino acid, arranged in. On one side of the spiral, all the charged amino acid residues are arranged on the other side. When 2 protein molecules are arranged in parallel, the leucine interacts to form a two poly body, forming a "zipper". In the "zipper"-type protein molecule, the amino acid form of the charge in addition to the leucine binds to the DNA.