This title appears in the Scientific Report :
2018
Please use the identifier:
http://hdl.handle.net/2128/17639 in citations.
Please use the identifier: http://dx.doi.org/10.1038/srep44297 in citations.
High-efficient production and biophysical characterisation of nicastrin, and ist interaction with APPC100
High-efficient production and biophysical characterisation of nicastrin, and ist interaction with APPC100
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...
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Personal Name(s): | Yu, Kun |
---|---|
Yang, Ge / Labahn, Jörg (Corresponding author) | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | Scientific reports, 7 (2017) S. 44297 |
Imprint: |
London
Nature Publishing Group
2017
|
DOI: |
10.1038/srep44297 |
Document Type: |
Journal Article |
Research Program: |
Functional Macromolecules and Complexes |
Link: |
OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1038/srep44297 in citations.
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. |