Leucine zippers are a dimerization motif of the bZIP (Basic-region leucine zipper) class of eukaryotic transcription factors. [3] The bZIP domain is 60 to 80 amino acids in length with a highly conserved DNA binding basic region and a more …

The coiled-coil protein motif, formed by leucine zipper peptides, is found in many natural proteins. Leucine zippers are characterized by a heptad repeat of the form abcdefg, where a and d are hydrophobic residues (d is often leucine) and e and g are charged residues.

A leucine zipper is an amphipathic helix in which every seventh amino acid is a leucine protruding from the hydrophobic face, with four to five repeats of this motif per protein (called bZIP proteins).

Homeodomain-leucine zipper (HD-Zip) proteins are transcription factors unique to plants and are encoded by more than 25 genes in Arabidopsis thaliana. Based on sequence analyses these proteins have been classified into four distinct groups: HD-Zip I–IV.

One form of DNA-binding motif is referred to as a leucine zipper. An example of a leucine zipper is a domain of protein GCN4. GCN4 is a 281-amino acid polypeptide, of which only the last 33 residues are required for dimerization.

CREB/CREM/ATF-1, Fos and Jun, and C/EBPβ, are basic leucine zipper (bZIP) proteins that bind to specific double-stranded DNA sequences as homodimers and/or heterodimers, and result in varying effects on transcription (Montminy et al., 1986; Meyer and Habener, 1993; Montminy, 1997; De Cesare and Sassone-Corsi, 2000; Shaulian and Karin, 2001 ...

In many eukaryotic gene regulatory proteins, the ZIP motif is flanked at its N-terminus by a basic region containing characteristic residues that facilitate DNA binding. A structure referred to as the leucine zipper or simply as ZIP has been proposed to explain how a class of eukaryotic gene regulatory proteins works (Landschulz et al., 1988).

The leucine zipper is a protein–protein interaction domain consisting of amphipathic a helices that dimerize in parallel, either as homodimers or heterodimers, to form a coiled-coil. The leucine zipper is the dimerization domain of the B-ZIP (basic-region leucine zipper) class of eukaryotic transcrip-tion factors (Vinson et al., 1989).

bZIP proteins are transcription factors that consist of three modular functional regions mediating dimerization, DNA binding and transcriptional regulation. The hallmark of these proteins is the bZIP (basic region, leucine zipper) domain, a well-defined motif in eukaryotic proteins (1, 2).

The contribution of the two Glu-70···Arg-73 ionic bonds to the thermodynamic stability of the GCN4 leucine zipper has been evaluated experimentally through protein engineering. The double mutant, E70A/R73A , has a melting temperature of 35 °C …