PROSITE documentation PDOC00029Leucine 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.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Landschulz W.H. Johnson P.F. McKnight S.L. |
| Title | The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins. | |
| Source | Science 240:1759-1764(1988). | |
| PubMed ID | 3289117 |
| 2 | Authors | Busch S.J. Sassone-Corsi P. |
| Title | Dimers, leucine zippers and DNA-binding domains. | |
| Source | Trends Genet. 6:36-40(1990). | |
| PubMed ID | 2186528 |
| 3 | Authors | O'Shea E.K. Rutkowski R. Kim P.S. |
| Source | Science 243:538-542(1989). |
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