X-ray scattering indicates that the leucine zipper is a coiled coil.
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منابع مشابه
X-ray scattering indicates that the leucine zipper is a coiled coil.
Dimerization of the bZIP class of eukaryotic transcriptional control proteins requires a sequence motif called the leucine zipper. We have grown two distinct crystal forms of a 33-amino acid peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4. This peptide is known to form a dimer of parallel helices in solution. X-ray scattering from both crystal forms shows...
متن کاملEvidence that the leucine zipper is a coiled coil.
Recently, a hypothetical structure called a leucine zipper was proposed that defines a new class of DNA binding proteins. The common feature of these proteins is a region spanning approximately 30 amino acids that contains a periodic repeat of leucines every seven residues. A peptide corresponding to the leucine zipper region of the yeast transcriptional activator GCN4 was synthesized and chara...
متن کاملX-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil.
The x-ray crystal structure of a peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4 has been determined at 1.8 angstrom resolution. The peptide forms a parallel, two-stranded coiled coil of alpha helices packed as in the "knobs-into-holes" model proposed by Crick in 1953. Contacts between the helices include ion pairs and an extensive hydrophobic interface t...
متن کاملSubdomain folding of the coiled coil leucine zipper from the bZIP transcriptional activator GCN4.
One popular model for protein folding, the framework model, postulates initial formation of secondary structure elements, which then assemble into the native conformation. However, short peptides that correspond to secondary structure elements in proteins are often only marginally stable in isolation. A 33-residue peptide (GCN4-p1) corresponding to the GCN4 leucine zipper folds as a parallel, t...
متن کاملPeriodicity of amide proton exchange rates in a coiled-coil leucine zipper peptide.
The two-stranded coiled-coil motif, which includes leucine zippers, is a simple protein structure that is well suited for studies of helix-helix interactions. The interaction between helices in a coiled coil involves packing of "knobs" into "holes", as predicted by Crick in 1953 and confirmed recently by X-ray crystallography for the GCN4 leucine zipper [O'Shea, E.K., Klemm, J.D., Kim, P.S., & ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1991
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.88.2.561