What is the Origin of Leucine Zipper?

This term was coined in the late 1980s following the discovery of its characteristic structure in several oncogene products and transcriptional regulators. The name is descriptive, combining 'leucine,' the amino acid that appears every seven residues, with 'zipper,' which describes the interdigitation of the two helical chains. It represents a major class of protein-protein interaction domains.

What is the Mechanism of Leucine Zipper?

The leucine zipper functions as a dimerization domain, where the interdigitation of the leucine residues from two separate protein monomers forms a stable, coiled-coil structure. Immediately adjacent to this dimerization domain is a region rich in basic amino acids that forms the DNA-binding domain. The dimerization is a prerequisite for the protein to bind to its specific DNA sequence, allowing the hormone-regulated transcription factor to control the expression of target genes and modulate cellular function.

Leucine Zipper ∞ Area

Leucine Zipper

Meaning

A Leucine Zipper is a common structural motif found in a family of DNA-binding proteins, including numerous transcription factors that regulate gene expression. This structure consists of two alpha-helical protein chains that dimerize, resembling a zipper due to a periodic repetition of the hydrophobic amino acid leucine. It is a critical component in the machinery that translates hormonal signals into genetic changes.