leucine zipper

(redirected from Leucine zipper domain)

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 ?
Using protein domain prediction tools on horse XBP1 protein sequences showed that the unchanged part of XBP1 contains a basic leucine zipper domain. We could predict any domain based on the C-terminal part of horse sXBP1 (Figure 3C), however, based on the protein sequence homology of horse sXBP1, it is reasonable to assume that the replaced part of the C-terminal has a transcription activator domain.
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].
Few years ago Li et al characterized in Nrf2 a nuclear export signal (NES) in the leucine zipper domain (NESzip) (25) and in the Neh5 transactivation domain ([NES.sub.TA]) (26).

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