%0 Journal Article
%A Yu, Kun
%A Yang, Ge
%A Labahn, Jörg
%T High-efficient production and biophysical characterisation of nicastrin, and ist interaction with APPC100
%J Scientific reports
%V 7
%@ 2045-2322
%C London
%I Nature Publishing Group
%M FZJ-2017-01837
%P 44297
%D 2017
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000395977600001
%R 10.1038/srep44297
%U https://juser.fz-juelich.de/record/827731