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PROSITE documentation PDOC00029 |
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:
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). |