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

Autor:	E C van Kappel, Madelon M. Maurice, Marc Baldus, Mark Daniëls, Meaghan E. Ward
Rok vydání:	2018
Předmět:	0301 basic medicine Amyloid Magnetic Resonance Spectroscopy Protein domain Plasma protein binding Catalysis Cofactor Protein–protein interaction 03 medical and health sciences Axin Protein Protein Domains Materials Chemistry Humans Binding site Wnt Signaling Pathway Binding Sites biology Chemistry Phosphatidylethanolamines Metals and Alloys Wnt signaling pathway General Chemistry Nuclear magnetic resonance spectroscopy Peptide Fragments 3. Good health Surfaces Coatings and Films Electronic Optical and Magnetic Materials 030104 developmental biology Solid-state nuclear magnetic resonance Ceramics and Composites Biophysics biology.protein Protein Binding
Zdroj:	Chemical Communications. 54:3959-3962
ISSN:	1364-548X 1359-7345
DOI:	10.1039/c8cc01346b
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ad3bdde0a1422a6c9d9d369ea35caf2 https://doi.org/10.1039/c8cc01346b Zobrazit plný text záznamu