leucine zipper


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leu·cine zip·per

a structural motif found in a number of proteins (for example, some of the DNA-binding regulatory proteins) in which leucyl residues align along one edge of the helix and can interdigitate with a similar structure on another protein molecule.
[Zipper, orig. a trademark for a fastening device with two rows of interlocking teeth]
References in periodicals archive ?
XBP1, X-box binding protein 1; sXBP1, spliced XBP1; usXBP1, un-spliced XBP1; Pit-1a, POU class 1 homeobox 1; ATF, activating transcription factor; bZIP, basic leucine zipper domain; aa, amino acid.
(1996) Bach proteins belong to a novel family of BTB-basic leucine zipper transcription factors that interact with MafK and regulate transcription through the NF-E2 site.
All these proteins share cap 'n' collar (CNC) and a basic leucine zipper (bZIP) domains in their C-terminus region.
The first leucine of the leucine zipper region was designed as +1, and C-terminal amino acid of the hinge region was numbered -1 [55].
Amino acids present at positions a, d, e, and g near the leucine zipper interface play an important role in regulating oligomerization of leucine zipper domain as well as specificity and stability of dimerization [4].
Isolation of NF E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region.
Nrf2 Possesses a redox-insensitive nuclear export signal overlapping with the leucine zipper motif.
Scissors-grip model for DNA recognition by a family of leucine zipper proteins.
In 1988, McKnight named this hydrophobic section the leucine zipper because he and his colleagues thought the leucines from two proteins lined up in such a way that they interlocked like teeth in a zipper.

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