Investigations of dynamic amyloid-like structures of the Wnt signalling pathway by solid-state NMR

Chem Commun (Camb). 2018 Apr 17;54(32):3959-3962. doi: 10.1039/C8CC01346B.


We report solid-state Nuclear Magnetic Resonance (ssNMR) studies on amyloid-like protein complexes formed by DIX domains that mediate key protein interactions in the Wnt signalling pathway. Our results provide insight into the 3D fold of the self-associated Axin-DIX domain and identify a potential lipid cofactor.

MeSH terms

  • Amyloid / chemistry*
  • Axin Protein / chemistry*
  • Axin Protein / metabolism
  • Binding Sites
  • Humans
  • Magnetic Resonance Spectroscopy
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism
  • Phosphatidylethanolamines / chemistry
  • Phosphatidylethanolamines / metabolism
  • Protein Binding
  • Protein Domains
  • Wnt Signaling Pathway*


  • Amyloid
  • Axin Protein
  • Peptide Fragments
  • Phosphatidylethanolamines