NMR solution structure of a highly stable de novo heterodimeric coiled‐coil

@article{Lindhout2004NMRSS,
  title={NMR solution structure of a highly stable de novo heterodimeric coiled‐coil},
  author={D. Lindhout and J. Litowski and P. Mercier and R. Hodges and B. Sykes},
  journal={Biopolymers},
  year={2004},
  volume={75}
}
The NMR solution structure of a highly stable coiled‐coil IAAL‐E3/K3 has been solved. The E3/K3 coiled‐coil is a 42‐residue de novo designed coiled‐coil comprising three heptad repeats per subunit, stabilized by hydrophobic contacts within the core and electrostatic interactions at the interface crossing the hydrophobic core which direct heterodimer formation. This E3/K3 domain has previously been shown to have high α‐helical content as well as possessing a low dissociation constant (70 nM… Expand
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References

SHOWING 1-10 OF 58 REFERENCES
Improving coiled-coil stability by optimizing ionic interactions.
TLDR
By combining the most favorable inter- and intrahelical salt-bridge arrangements it is possible to design coiled-coil oligomerization domains with improved stability properties and the rational design principles are verified by comparing this structure to the structure of the parent peptide. Expand
Removing an interhelical salt bridge abolishes coiled-coil formation in a de novo designed peptide.
TLDR
It is shown that the peptide, while being highly alpha-helical, is no longer able to form a parallel coiled-coil structure but rather assumes an octameric globular helical assembly devoid of any coiled -coil interactions. Expand
The role of position a in determining the stability and oligomerization state of α‐helical coiled coils: 20 amino acid stability coefficients in the hydrophobic core of proteins
TLDR
It is found that nine of the analogs populated one oligomerization state exclusively at peptide concentrations of 50 μM under benign buffer conditions, and the Leu‐, Tyr‐, Gln‐, and His‐substituted analogs were found to be exclusively three‐stranded trimers, while the Asn-, Lys‐, Orn‐, Arg‐, Trp‐ Substituting analogs formed exclusively two-stranded monomers. Expand
Use of a heterodimeric coiled-coil system for biosensor application and affinity purification.
TLDR
The universality of coiled-coil as a dimerization motif in nature and the ability to design and synthesize these proteins suggest a wide variety of applications. 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
Coiled coils: a highly versatile protein folding motif.
TLDR
This highly versatile protein folding and oligomerization motif is discussed with regard to its structural architecture and how this is related to its biological functions. Expand
High Resolution NMR Solution Structure of the Leucine Zipper Domain of the c-Jun Homodimer*
The solution structure of the c-Jun leucine zipper domain has been determined to high resolution using a new calculation protocol designed to handle highly ambiguous sets of interproton distanceExpand
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
A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions.
TLDR
A thermodynamic scale (delta delta G) for 27 interhelical interactions in 35 proteins between amino acids in the g and the following e positions of a leucine zipper coiled coil indicates that E<==>R is the most stable interhelICAL pair. Expand
Crystal structure of an isoleucine-zipper trimer
SUBUNIT oligomerization in many proteins is mediated by short coiled-coil motifs1,2. These motifs share a characteristic seven-amino-acid repeat containing hydrophobic residues at the first (a) andExpand
...
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2
3
4
5
...