{PDOC00029}
{PS00029; LEUCINE_ZIPPER}
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* Leucine zipper pattern *
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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 alpha-helical
conformation. The leucine side chains extending from one alpha-helix  interact
with those  from a similar alpha 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).

-Consensus pattern: L-x(6)-L-x(6)-L-x(6)-L
-Sequences known to belong to this class detected by the pattern: All    those
 mentioned in the original paper, with the exception of L-myc which  has a Met
 instead of the second Leu.
-Other sequence(s) detected in Swiss-Prot: some 600 other sequences from every
 category of protein families.

-Note: 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.

[ 1] Landschulz W.H., Johnson P.F., McKnight S.L.
     "The leucine zipper: a hypothetical structure common to a new class of
     DNA binding proteins."
     Science 240:1759-1764(1988).
     PubMed=3289117
[ 2] Busch S.J., Sassone-Corsi P.
     "Dimers, leucine zippers and DNA-binding domains."
     Trends Genet. 6:36-40(1990).
     PubMed=2186528
[ 3] O'Shea E.K., Rutkowski R., Kim P.S.
     Science 243:538-542(1989).

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