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

Biopolymers. 2004 Dec 5;75(5):367-75. doi: 10.1002/bip.20150.


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 alpha-helical content as well as possessing a low dissociation constant (70 nM). The E3/K3 structure is completely alpha-helical and is an archetypical coiled-coil in solution, as determined using a combination of (1)H-NOE and homology based structural restraints. This structure provides a structural framework for visualizing the important interactions for stability and specificity, which are key to protein engineering applications such as affinity purification and de novo design.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • DNA-Binding Proteins / chemistry*
  • Helix-Turn-Helix Motifs
  • Magnetic Resonance Spectroscopy
  • Models, Molecular*
  • Molecular Sequence Data
  • Peptides / chemistry
  • Protein Structure, Tertiary


  • DNA-Binding Proteins
  • Peptides