Leucine Zipper
نویسندگان
چکیده
The leucine zipper is the dimerization domain of the B-ZIP (basic-region leucine zipper) class of eukaryotic transcription factors (Vinson et al., 1989). The name arose because leucines occur every seven amino acids in this dimerization domain.These leucines are critical for the dimerization and DNA binding of B-ZIP proteins. The leucine zipper is a left-handed parallel dimeric coiled-coil, a structure proposed independently by Pauling and Corey, and by Crick in 1953.
منابع مشابه
Structure of homeobox-leucine zipper genes suggests a model for the evolution of gene families.
Homeobox genes are present in both plants and animals. Homeobox-leucine zipper genes, however, have been identified thus far only in the small mustard plant Arabidopsis thaliana. This observation suggests that homeobox-leucine zipper genes evolved after the divergence of plants and animals, perhaps to mediate specific regulatory events. To better understand this gene family, we isolated several...
متن کاملA leucine zipper motif essential for gating of hyperpolarization-activated channels.
BACKGROUND It is poorly understood how hyperpolarization-activated cyclic nucleotide-gated channels (HCNs) function. RESULTS We have identified a leucine zipper in the S5 segment of HCNs, regulating hyperpolarization-activated and instantaneous current components. CONCLUSION The leucine zipper is essential for HCN channel gating. SIGNIFICANCE The identification and functional characteriza...
متن کاملHelical supramolecules and fibers utilizing leucine zipper-displaying dendrimers.
We describe a new family of discrete supramolecules comprising leucine-zipper peptides noncovalently assembled upon cognate leucine zippers fused to a dendrimer core. Circular dichroism and sedimentation equilibrium experiments clearly demonstrate that each leucine-zipper dendrimer (D-EZ4 or D-KZ4) can noncovalently display four leucine zippers on their surface that can be utilized for the mult...
متن کاملThe leucine zipper of TFE3 dictates helix-loop-helix dimerization specificity.
TFE3 is a DNA-binding protein that activates transcription through the muE3 site of the immunoglobulin heavy-chain enhancer. Its amino acid sequence reveals two putative protein dimerization motifs: a helix-loop-helix (HLH) and an adjacent leucine zipper. We show here that both of these motifs are necessary for TFE3 to homodimerize and to bind DNA in vitro. Using a dominant negative TFE3 mutant...
متن کاملPredicting leucine zipper structures from sequence.
The leucine zipper structure is adopted by one family of the coiled coil proteins. Leucine zippers have a characteristic leucine repeat: Leu-X6-Leu-X6-Leu-X6-Liu (where X may be any residue). However, many sequences have the leucine repeat, but do not adopt the leucine zipper structure (we shall refer to these as non-zippers). We have found and analyzed residue pair patterns that allow one to i...
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تاریخ انتشار 2001