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.
The leucine zipper usually consists of a short string of amino acids embedded within a long protein.
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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