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

M E Ward; M A Daniëls; E C van Kappel; M M Maurice; M Baldus

doi:10.1039/C8CC01346B

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

M E Ward, M A Daniëls, E C van Kappel, M M Maurice, M Baldus

Research output: Contribution to journal › Article › Academic › peer-review

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.

Original language	English
Pages (from-to)	3959-3962
Number of pages	4
Journal	Chemical Communications
Volume	54
Issue number	32
DOIs	https://doi.org/10.1039/C8CC01346B
Publication status	Published - 17 Apr 2018

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title = "Investigations of dynamic amyloid-like structures of the Wnt signalling pathway by solid-state NMR",

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.",

author = "Ward, {M E} and Dani{\"e}ls, {M A} and {van Kappel}, {E C} and Maurice, {M M} and M Baldus",

note = "Publisher Copyright: {\textcopyright} 2018 The Royal Society of Chemistry.",

year = "2018",

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AU - Ward, M E

AU - Daniëls, M A

AU - van Kappel, E C

AU - Maurice, M M

AU - Baldus, M

PY - 2018/4/17

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N2 - 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.

AB - 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.

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DO - 10.1039/C8CC01346B

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JO - Chemical Communications

JF - Chemical Communications

IS - 32

ER -

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

Abstract

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