Leucine Zipper

A leucine zipper, aka leucine scissors, is a common three-dimensional structural motif in proteins. These motifs are usually found as part of a DNA-binding domain in various transcription factors, and are therefore involved in regulating gene expression. Leucine zippers are found in both eukaryotic and prokaryotic regulatory proteins, but are mainly a feature of eukaryotes.

The leucine zipper is a super-secondary structure that functions as a dimerization domain, and its presence generates adhesion forces in parallel alpha helices. A single leucine zipper consists of multiple leucine residues at approximately 7-residue intervals, which forms an amphipathic alpha helix with a hydrophobic region running along one side. This hydrophobic region provides an area for dimerization, allowing the motifs to "zip" together. Furthermore, the hydrophobic leucine region is absolutely required for DNA binding.

Read more about Leucine ZipperStructure, Biology

Other articles related to "leucine zipper, zipper":

Leucine Zipper - Biology
... Leucine zipper regulatory proteins include c-fos and c-jun (the AP1 transcription factor), important regulators of normal development, as well as myc family members ... interact with the DNA as dimers (homo- or hetero-) and are also called basic zipper proteins (bZips) ...
Ccaat-enhancer-binding Proteins
... They are characterized by a highly conserved basic-leucine zipper (bZIP) domain at the C-terminus ... and DNA binding like other transcription factors of the leucine zipper domain-containing family (i.e ... factors that may or may not contain the leucine zipper domain ...
Bimolecular Fluorescence Complementation - History
... system that allowed a green fluorescent protein (GFP) to be reassembled using an anti-parallel leucine zipper in E ... As the GFP fragment was attached to each leucine zipper by a linker, the heterodimerisation of the anti-parallel leucine zipper resulted in a reconstituted, or re-formed, GFP protein ...