{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7"],"submitter":["Yu K"],"pubmed_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."],"journal":["Scientific reports"],"pagination":["44297"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5343570"],"repository":["biostudies-literature"],"pubmed_title":["High-efficient production and biophysical characterisation of nicastrin and its interaction with APPC100."],"pmcid":["PMC5343570"],"pubmed_authors":["Yang G","Labahn J","Yu K"],"additional_accession":[]},"is_claimable":false,"name":"High-efficient production and biophysical characterisation of nicastrin and its interaction with APPC100.","description":"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.","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Mar","modification":"2025-04-04T14:32:55.613Z","creation":"2019-03-27T02:38:16Z"},"accession":"S-EPMC5343570","cross_references":{"pubmed":["28276527"],"doi":["10.1038/srep44297"]}}