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^*

^*Corresponding author for this work

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
Journal	Chemical Communications
Volume	54
Issue number	32
DOIs	https://doi.org/10.1039/C8CC01346B
Publication status	Published - 2018

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c8cc01346bFinal published version, 3.15 MBLicence: Taverne

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@article{3700ffdcdf0045aebec0eb8a838bbde0,

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",

year = "2018",

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language = "English",

volume = "54",

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journal = "Chemical Communications",

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publisher = "Royal Society of Chemistry",

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AU - Daniëls, M. A.

AU - Van Kappel, E. C.

AU - Maurice, M. M.

AU - Baldus, M.

PY - 2018

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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.

U2 - 10.1039/C8CC01346B

DO - 10.1039/C8CC01346B

M3 - Article

SN - 1359-7345

VL - 54

SP - 3959

EP - 3962

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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