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Chem Commun (Camb) ; 54(32): 3959-3962, 2018 Apr 17.
Article in English | MEDLINE | ID: mdl-29561051

ABSTRACT

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.


Subject(s)
Amyloid/chemistry , Axin Protein/chemistry , Peptide Fragments/chemistry , Wnt Signaling Pathway , Axin Protein/metabolism , Binding Sites , Humans , Magnetic Resonance Spectroscopy , Peptide Fragments/metabolism , Phosphatidylethanolamines/chemistry , Phosphatidylethanolamines/metabolism , Protein Binding , Protein Domains
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