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

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 l...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2018, Vol.54 (32), p.3959-3962
Main Authors: Ward, M E, Daniëls, M A, van Kappel, E C, Maurice, M M, Baldus, M
Format: Article
Language:English
Subjects:
NMR
Nuclear magnetic resonance
Signaling
Solid state
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Summary: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.
ISSN:1359-7345
1364-548X
DOI:10.1039/c8cc01346b