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a white crystalline amino acid occurring in proteins that is essential for nutrition; obtained by the hydrolysis of most dietary proteins

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/09/05 09:45:06」(JST)

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"Overhead view", or helical wheel diagram, of a leucine zipper, where d represent amino acid leucine, arranged with other amino acids on two parallel alpha helices.

A leucine zipper, aka leucine scissors,^[1] is a common three-dimensional structural motif in proteins. These motifs are usually found as part of a DNA-binding domain in various transcription factors, and are therefore involved in regulating gene expression. Leucine zippers are found in both eukaryotic and prokaryotic regulatory proteins, but are mainly a feature of eukaryotes.

The leucine zipper is a super-secondary structure that functions as a dimerization domain, and its presence generates adhesion forces in parallel alpha helices.^[2] A single leucine zipper consists of multiple leucine residues at approximately 7-residue intervals, which forms an amphipathic alpha helix with a hydrophobic region running along one side. This hydrophobic region provides an area for dimerization, allowing the motifs to "zip" together. Furthermore, the hydrophobic leucine region is absolutely required for DNA binding.

Structure[edit source | edit]

Leucine Zipper (blue) bound to DNA. The leucine residues that represent the 'teeth' of the zipper are colored red

The main feature of the leucine zipper domain is the predominance of the common amino acid leucine at the d position of the heptad repeat. Leucine zippers were first identified by sequence alignment of certain transcription factors that identified a common pattern of leucines every seven amino acids. These leucines were later shown to form the hydrophobic core of a coiled coil.

Each half of a leucine zipper consists of a short alpha-helix with a leucine residue at every seventh position. The standard 3.6-residues-per-turn alpha-helix structure changes slightly to become a 3.5-residues-per-turn alpha-helix. Known also as the heptad repeat, one leucine comes in direct contact with another leucine on the other strand every second turn.

The bZIP family of transcription factors consists of a basic region that interacts with the major groove of a DNA molecule through hydrogen bonding, and a hydrophobic leucine zipper region that is responsible for dimerization.

Biology[edit source | edit]

Leucine zipper regulatory proteins include c-fos and c-jun (the AP1 transcription factor), important regulators of normal development, as well as myc family members including myc, max, and mdx1. If they are overproduced or mutated in a vital area, they may generate cancer. These proteins interact with the DNA as dimers (homo- or hetero-) and are also called basic zipper proteins (bZips).

References[edit source | edit]

^ David M. Glick, ed. (1997). "Leucine scissors". Glossary of Biochemistry and Molecular Biology (Revised ed.). London: Portland Press.
^ Landschulz WH, Johnson PF, McKnight SL (1988-06-24). "The leucine zipper: a hypothetical structure common to a new class of DNA-binding proteins". Science 240 (4860): 1759–1764. doi:10.1126/science.3289117. PMID 3289117.

External links[edit source | edit]

Leucine zippers at the US National Library of Medicine Medical Subject Headings (MeSH)

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Failure to Target RANKL Signaling Through p38-MAPK Results in Defective Osteoclastogenesis in the Microphthalmia Cloudy-Eyed Mutant.

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PMID 26218069

Basic leucine zipper (bZIP) transcription factors involved in abiotic stresses: A molecular model of a wheat bZIP factor and implications of its structure in function.

Sornaraj P1, Luang S1, Lopato S1, Hrmova M2.
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BACKGROUND: Basic leucine zipper (bZIP) genes encode transcription factors (TFs) that control important biochemical and physiological processes in plants and all other eukaryotic organisms.SCOPE OF REVIEW: Here we present (i) the homo-dimeric structural model of bZIP consisting of basic leucine zipp
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High affinity receptor labeling based on basic leucine zipper domain peptides conjugated with pH-sensitive fluorescent dye: Visualization of AMPA-type glutamate receptor endocytosis in living neurons.

Hayashi A1, Asanuma D2, Kamiya M3, Urano Y3, Okabe S4.
Neuropharmacology.Neuropharmacology.2016 Jan;100:66-75. doi: 10.1016/j.neuropharm.2015.07.026. Epub 2015 Jul 26.
Techniques to visualize receptor trafficking in living neurons are important, but currently available methods are limited in their labeling efficiency, specificity and reliability. Here we report a method for receptor labeling with a basic leucine zipper domain peptide (ZIP) and a binding cassette s
PMID 26220312

Japanese Journal

Critical role of JSAP1 and JLP in axonal transport in the cerebellar Purkinje cells of mice

FEBS Letters 589(19), 2805-2811, 2015-07-03
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A novel in-frame deletion in the leucine zipper domain of C/EBPε leads to neutrophil-specific granule deficiency

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Generation and characterization of MafA-Kusabira Orange mice

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リンク元	「ロイシンジッパー」
拡張検索	「basic-leucine zipper transcription factor」「basic helix-loop-helix leucine zipper transcription factor」「leucine zipper domain」
関連記事	「zipper」