Journal Article

FZJ-2017-01837

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png High-efficient production and biophysical characterisation of nicastrin, and ist interaction with APPC100

Yu, K. ; Yang, G.FZJ* ; Labahn, J. (Corresponding author)FZJ*

2017
Nature Publishing Group London

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Please use a persistent id in citations: http://hdl.handle.net/2128/17639  doi:10.1038/srep44297

Abstract: Nicastrin, the largest member among the four components of the γ-secretase complex, has been identified to be the substrate recognizer for the proteolytic activity of the complex. Here we report that full-length human nicastrin (hNCT) can be obtained by heterologous expression in E. coli. Milligram quantities of the target protein are purified in a two-step purification protocol using affinity chromatography followed by SEC. The FOS-choline 14 purified tetrameric hNCT exhibits a proper folding with 31% α-helix and 23% β-sheet content. Thermal stability studies reveal stable secondary and tertiary structure of the detergent purified hNCT. A physical interaction between nicastrin and the γ-secretase substrate APPC100 confirmed the functionality of hNCT as a substrate recognizer.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 551 - Functional Macromolecules and Complexes (POF3-551) (POF3-551)

Appears in the scientific report 2018

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