Crystal structure of leucine zipper protein Hy5 complexed with DNA
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چکیده
منابع مشابه
Crystal Structure of the Oxytricha nova Telomere End Binding Protein Complexed with Single Strand DNA
Telomeres are specialized protein-DNA complexes that compose the ends of eukaryotic chromosomes. Telomeres protect chromosome termini from degradation and recombination and act together with telomerase to ensure complete genome replication. We have determined the crystal structure of the two-subunit Oxytricha nova telomere end binding protein (OnTEBP) complexed with single strand telomeric DNA ...
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Rat liver chromatin was titrated by poly-D-lysine of mol.wt. 140,000. Approximately 32% of the phosphate groups of the chromatin were found to react with the polycation. By submitting the chromatin-poly-D-lysine complex to pronase and DNase I digestion and by further submitting the obtained DNA-lysine complex to hydroxy-apatite-chromatography, “free” DNA was isolated. The mean S-value of this D...
متن کاملThe GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex.
The yeast transcriptional activator GCN4 is 1 of over 30 identified eukaryotic proteins containing the basic region leucine zipper (bZIP) DNA-binding motif. We have determined the crystal structure of the GCN4 bZIP element complexed with DNA at 2.9 A resolution. The bZIP dimer is a pair of continuous alpha helices that form a parallel coiled coil over their carboxy-terminal 30 residues and grad...
متن کاملLeucine Zipper
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 s...
متن کاملLeucine Zipper Mutants
Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residues were altered, two-, three-, and four-helix structures were formed. The x-ray crystal structure of ...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 2005
ISSN: 0108-7673
DOI: 10.1107/s0108767305090513