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

M E WardM A DaniëlsE C van KappelMadelon M MauriceMarc Baldus
Published in: Chemical communications (Cambridge, England) (2018)
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.
Keyphrases
  • solid state
  • magnetic resonance
  • cell proliferation
  • stem cells
  • high resolution
  • protein protein
  • contrast enhanced
  • case control
  • amino acid
  • binding protein
  • fatty acid
  • human health
  • risk assessment