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]


Leu; a naturally occurring amino acid, essential for growth in the young and for nitrogen equilibrium in adults.

leucine aminopeptidase
a digestive enzyme of small intestine enterocytes (brush border).
synthetic form of leucine.
leucine enkephalin
leu-enkephalin; see enkephalin.
natural form of leucine.
leucine zipper
a structured motif found in some DNA binding regulatory proteins formed from a region of α-helix containing at least four leucines, each separated by six amino acids from one another; the leucines align along one edge of the α-helix with one leucine at every second turn of the helix such that the leucine of one protein can interdigitate with the leucines of another protein in a zipper manner.
References in periodicals archive ?
Leucine zippers are employed to mediate dimerization of scFv in a miniantibody form.
The new work also clarifies the atomic nature of so-called leucine zippers stretches of amino acids that bind two proteins into two-molecule complexes called dimers, which regulate gene activity Confirmation that leucine zippers are actually coiled coils will help scientists understand how these proteins regulate the on-and-off switching of genes, comments Steven L.
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.
Sometimes the leucine zipper helps two different molecules link up, says Kim.

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