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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...

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Identifiers

PMID: 29109152
DOI: 10.1074/jbc.M117.809657
PMCID: PMC5798290

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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