Surface salt bridges stabilize the GCN4 leucine zipper
نویسندگان
چکیده
منابع مشابه
An intrahelical salt bridge within the trigger site stabilizes the GCN4 leucine zipper.
We previously reported that a helical trigger segment within the GCN4 leucine zipper monomer is indispensable for the formation of its parallel two-stranded coiled coil. Here, we demonstrate that the intrinsic secondary structure of the trigger site is largely stabilized by an intrahelical salt bridge. Removal of this surface salt bridge by a single amino acid mutation induced only minor change...
متن کاملMeasurement of interhelical electrostatic interactions in the GCN4 leucine zipper.
The dimerization specificity of the bZIP transcription factors resides in the leucine zipper region. It is commonly assumed that electrostatic interactions between oppositely charged amino acid residues on different helices of the leucine zipper contribute favorably to dimerization specificity. Crystal structures of the GCN4 leucine zipper contain interhelical salt bridges between Glu20 and Lys...
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 کاملDe novo simulations of the folding thermodynamics of the GCN4 leucine zipper.
Entropy Sampling Monte Carlo (ESMC) simulations were carried out to study the thermodynamics of the folding transition in the GCN4 leucine zipper (GCN4-lz) in the context of a reduced model. Using the calculated partition functions for the monomer and dimer, and taking into account the equilibrium between the monomer and dimer, the average helix content of the GCN4-lz was computed over a range ...
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Basic-region leucine zipper (bZIP) proteins are one of the largest transcription factor families that regulate a wide range of cellular functions. Owing to the stability of their coiled coil structure leucine zipper (LZ) domains of bZIP factors are widely employed as dimerization motifs in protein engineering studies. In the course of one such study, the X-ray structure of the retro-version of ...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1998
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.5560071121