Leucine Zipper motif

The leucine zipper motif (bZip) mediates both DNA binding and dimerization.

The structure of Leucine Zipper motif:

1. Two distinct right handed α helices participate in the formation of homo-or heterodimer structure.
2. N-terminal DNA binding domain is rich in positively charged amino acid residues.
3. C-terminal dimerization domain is approximately 30-40 amino acids long with a leucine at every seventh position.
4. The two α-helices in parallel wind around each other to form a coiled structure.
5. The Leucine residues end up with their R-groups protruding from the α helical domain in which the leucine residues reside.
6. The protruding R groups are thought to interdigitate with leucine R groups of another leucine zipper domain, thus stabilizing homo- or heterodimerization.

Occurrence:

The Leucine zipper domain is present in many DNA binding proteins, such as c-Myc, Jun, Fos and C/EBP in mammals.

The diagrammatic representation of Leucine-Zipper motif:

Other DNA binding motifs:

1. Introduction to DNA binding motifs: https://thebiologyislove.com/dna-binding-motifs/
2. helix-turn-helix: https://thebiologyislove.com/helix-turn-helix-motif/
3. helix-loop-helix: https://thebiologyislove.com/helix-loop-helix-motif/
4. zinc finger motif: https://thebiologyislove.com/zinc-finger-motif-c2-h2/

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