Prodomain–growth factor swapping in the structure of pro-TGF-β1

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...

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Detalles Bibliográficos
Autores principales: Zhao, Bo, Xu, Shutong, Dong, Xianchi, Lu, Chafen, Springer, Timothy A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2018
Materias:
Protein Structure and Folding
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5798290/
https://www.ncbi.nlm.nih.gov/pubmed/29109152
http://dx.doi.org/10.1074/jbc.M117.809657

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5798290/
https://www.ncbi.nlm.nih.gov/pubmed/29109152
http://dx.doi.org/10.1074/jbc.M117.809657

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