TY  - JOUR
AU  - Yu, Kun
AU  - Yang, Ge
AU  - Labahn, Jörg
TI  - High-efficient production and biophysical characterisation of nicastrin, and ist interaction with APPC100
JO  - Scientific reports
VL  - 7
SN  - 2045-2322
CY  - London
PB  - Nature Publishing Group
M1  - FZJ-2017-01837
SP  - 44297
PY  - 2017
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000395977600001
DO  - DOI:10.1038/srep44297
UR  - https://juser.fz-juelich.de/record/827731
ER  -