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The leucine zipper of Fos mediates only heterodimerization; it cannot homodimerize
Jun, the oncoprotein. B-ZIP transcription factors (98) are exclusively eukaryotic proteins that bind to sequence-specific double-stranded DNA as homodimers or heterodimers to either activate or repress gene transcription (34). We have examined both of the recently published DNA sequences of the human genome (51, 95) and identified 56 genes that contain the B-ZIP motif. The leucine zipper of Fos mediates only heterodimerization; it cannot homodimerize. In contrast, the leucine zippers of GCN4 and of EB1 exclusively homodimerize and do not form dimers with other bZip proteins.
bZIP proteins are transcription factors that consist of three modular functional regions mediating dimerization, DNA binding and transcriptional regulation
bZIP proteins are transcription factors that consist of three modular functional regions mediating dimerization, DNA binding and transcriptional regulation. The hallmark of these proteins is the bZIP (basic region, leucine zipper) domain, a well-defined motif in eukaryotic proteins (1, 2). The basic region of the bZIP domain, rich in lysines and arginines, represents the DNA contact surface, interacting with the major groove of the DNA double helix. The zipper region is an amphipathic helix of 30–40 residues with every seventh residue a leucine
A leucine zipper (or leucine scissors) is a common three-dimensional structural motif in proteins
A leucine zipper (or leucine scissors) is a common three-dimensional structural motif in proteins. They were first described by Landschulz and collaborators in 1988 when they found that an enhancer binding protein had a very characteristic 30-amino acid segment and the display of these amino acid sequences on an idealized alpha helix revealed a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns.
Transcription factors 1: bZIP proteins. Hurst HC1. Author information. Molecular Sequence Data. Protein Conformation. Transcription Factors/chemistry. Transcription Factors/metabolism. Basic-Leucine Zipper Transcription Factors. DNA-Binding Proteins. G-Box Binding Factors. Transcription Factors.
Leucine zipper transcription factors contain leucine residues at every seventh position in the C-terminal end of the DNA-binding domains (DBDs). These proteins often function as dimers using two extended α-helices to bind DNA at two different major groves. Proteins in this class use basic residues in the α-helix to bind the phosphate groups present in the backbone of DNA in addition to interactions with specific base pairs of the major groove.
Basic-leucine zipper transcription factors. A leucine zipper, aka leucine scissors, 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.
This class includes the CREB/ATF family of transcription factors, namely CREB, cAMP response element modulator (CREM), ATF, and the related AP-1 and C/EBP families. An effort has been made to elucidate the role of specific bZIP members in the heart. Unfortunately, little insight could be gained from knockout experiments, either due to embryonic lethal phenotypes or functional compensation by other bZIP family members.
Known as: Basic-Leucine Zipper Transcription Factors, bZIP Protein, Transcription Factors .
Known as: Basic-Leucine Zipper Transcription Factors, bZIP Protein, Transcription Factors, bZIP. Bipartite DNA binding protein containing a basic region that directly interacts with DNA, and a leucine zipper that mediates dimerization throug. More). National Institutes of Health.
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Transcription factors are proteins that bind to regulatory elements on the DNA and have a significant role in the . The leucine-zipper (or the basic leucine zipper) domain contains an alpha helix with a leucine at every 7 th amino acid.
Transcription factors are proteins that bind to regulatory elements on the DNA and have a significant role in the regulation of gene expression. Hence, one domain of many transcription factors is a DNA-binding domain. Transcription factors can activate or repress gene expression The leucine-zipper (or the basic leucine zipper) domain contains an alpha helix with a leucine at every 7 th amino acid. If two leucine zipper domains find one another, the leucines can interact like the teeth in a zipper, allowing the dimerization of two proteins.