PROSITE documentation PDOC00029
Leucine zipper pattern


A structure, referred to as the 'leucine zipper' [1,2], has been proposed to explain how some eukaryotic gene regulatory proteins work. The leucine zipper consist of a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns. The segments containing these periodic arrays of leucine residues seem to exist in an α-helical conformation. The leucine side chains extending from one α-helix interact with those from a similar α helix of a second polypeptide, facilitating dimerization; the structure formed by cooperation of these two regions forms a coiled coil [3]. The leucine zipper pattern is present in many gene regulatory proteins, such as:

  • The CCATT-box and enhancer binding protein (C/EBP).
  • The cAMP response element (CRE) binding proteins (CREB, CRE-BP1, ATFs).
  • The Jun/AP1 family of transcription factors.
  • The yeast general control protein GCN4.
  • The fos oncogene, and the fos-related proteins fra-1 and fos B.
  • The C-myc, L-myc and N-myc oncogenes.
  • The octamer-binding transcription factor 2 (Oct-2/OTF-2).

As this is far from being a specific pattern you should be cautious in citing the presence of such pattern in a protein if it has not been shown to be a nuclear DNA-binding protein.

Last update:

December 1992 / Text revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

LEUCINE_ZIPPER, PS00029; Leucine zipper pattern  (PATTERN with a high probability of occurrence!)


1AuthorsLandschulz W.H. Johnson P.F. McKnight S.L.
TitleThe leucine zipper: a hypothetical structure common to a new class of DNA binding proteins.
SourceScience 240:1759-1764(1988).
PubMed ID3289117

2AuthorsBusch S.J. Sassone-Corsi P.
TitleDimers, leucine zippers and DNA-binding domains.
SourceTrends Genet. 6:36-40(1990).
PubMed ID2186528

3AuthorsO'Shea E.K. Rutkowski R. Kim P.S.
SourceScience 243:538-542(1989).

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