Coiled Coil Domains: Stability, Specificity, and Biological Implications

@article{Mason2004CoiledCD,
  title={Coiled Coil Domains: Stability, Specificity, and Biological Implications},
  author={Jody M. Mason and Katja M. Arndt},
  journal={ChemBioChem},
  year={2004},
  volume={5}
}
The coiled coil is a common structural motif, formed by approximately 3 ± 5% of all amino acids in proteins. Typically, it consists of two to five -helices wrapped around each other into a left-handed helix to form a supercoil. Whereas regular -helices go through 3.6 residues for each complete turn of the helix, the distortion imposed upon each helix within a left-handed coiled coil lowers this value to around 3.5. Thus a heptad repeat occurs every two turns of the helix. 3] The coiled coil was… Expand
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TLDR
It is argued that coiled coils are ideal subjects for studies of subtle and large-scale structural changes because of their well-characterized and versatile nature. Expand
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
The roles of the a and d "hydrophobic" core positions and the e and g "electrostatic" edge positions in directing oligomerization and pairing specificity are discussed. Expand
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Sliding Mechanism at a Coiled-Coil Interface.
TLDR
This study explains the sliding that has been experimentally observed for the antiparallel CC of the dynein stalk region and the nuclear pore complex and suggests that this one-dimensional motion is an intrinsic feature in CC systems that can be involved in other CC systems. Expand
Crystal structure of the central coiled-coil domain from human liprin-β2.
TLDR
It is found that the human liprin-β2 coiled-coil forms an extended dimer and a 2.0 Å crystal structure of the central, protease-resistant core of theliprin- β2 coil reveals a parallel helix orientation. Expand
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References

SHOWING 1-10 OF 75 REFERENCES
Coiled-coil assembly by peptides with non-heptad sequence motifs.
TLDR
The heptad paradigm for the coiled coil must be expanded to include hendecads to provide a mechanism to promote cognate protein pairings during the folding of extended coiled coils in the cell. Expand
Coiled-coils: stability, specificity, and drug delivery potential.
  • Y. Yu
  • Chemistry, Medicine
  • Advanced drug delivery reviews
  • 2002
TLDR
How knowledge on protein stability and specificity can be used in the de novo design of peptide-based drug delivery vehicles with well-defined structure and interaction features is illustrated. Expand
A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants.
TLDR
These studies demonstrate that conserved, buried residues in the GCN4 leucine zipper direct dimer formation are essential determinants of the global fold. Expand
Are trigger sequences essential in the folding of two-stranded alpha-helical coiled-coils?
TLDR
It is proposed that surpassing a critical threshold stability value using any type or combination of stabilizing effects will allow coiled-coils to fold, in the absence of a specific trigger sequence per se. Expand
A buried polar interaction can direct the relative orientation of helices in a coiled coil.
TLDR
It is demonstrated that a single buried polar interaction in the interface between the helices of a coiled coil is sufficient to determine the relative orientation of its constituent helices. Expand
An autonomous folding unit mediates the assembly of two-stranded coiled coils.
TLDR
A 13-residue sequence pattern that occurs with limited sequence variations in many two-stranded coiled coils and that is absolutely required for the assembly of the Dictyostelium discoideum actin-bundling protein cortexillin I and the yeast transcriptional activator GCN4 is reported. Expand
Designing Heterodimeric Two-stranded α-Helical Coiled-coils
The E/K coil, a heterodimeric coiled-coil, has been designed as a universal peptide capture and delivery system for use in applications such as biosensors and as an expression and affinityExpand
Complementation of buried lysine and surface polar residues in a designed heterodimeric coiled coil.
TLDR
It is shown that polar interactions involving buried position-a Lys residues that can interact favorably only with surface e' or g' Glu residues also impart structural uniqueness to a designed heterodimeric coiled coil with the nativelike properties of sigmoidal thermal and urea-induced unfolding transitions, slow hydrogen exchange and lack of ANS binding. Expand
Peptide ‘Velcro’: Design of a heterodimeric coiled coil
TLDR
The design of two peptides that are predominantly unfolded in isolation but which, when mixed, associate preferentially to form a stable, parallel, coiled-coil heterodimer show that it is possible to design peptides with simple sequences that have a very high preference to pair with one another. Expand
The role of interhelical ionic interactions in controlling protein folding and stability. De novo designed synthetic two-stranded alpha-helical coiled-coils.
TLDR
This study suggests that the folding process for these synthetic model coiled-coils does not involve a single-stranded alpha-helix as a significantly populated folding intermediate and demonstrates that a large number of these weak interactions can play an important role in the assembly of helices. Expand
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