Article
Prodomain-growth factor swapping in the structure of pro-TGF-β1.
The Journal of biological chemistry - 2 Feb 2018
Zhao Bo, Xu Shutong, Dong Xianchi, Lu Chafen, Springer Timothy A
Abstract excerpt
TGF-β is synthesized as a proprotein that dimerizes in the endoplasmic reticulum. After processing in the Golgi to cleave the N-terminal prodomain from the C-terminal growth factor (GF) domain in each monomer, pro-TGF-β is secreted and stored in latent complexes. It is unclear which prodomain and GF monomer are linked before proprotein convertase cleavage and how much conformational change occurs following...
Topics
- Golgi Apparatus
- HEK293 Cells
- Humans
- Models, Molecular
- Mutation
- Protein Domains
- Protein Precursors
- Transforming Growth Factor beta1