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TitleLatent-TGF-β has a domain swapped architecture.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 10469, Year 2025
Publish dateNov 25, 2025
AuthorsMingliang Jin / Robert I Seed / Tiffany Shing / Li Wang / Junrui Li / Yifan Cheng / Stephen L Nishimura /
PubMed AbstractThe multifunctional cytokine TGF-β is a dimeric protein produced within a latent complex (L-TGF-β). Latency is maintained by disulfide linked homodimeric prodomains forming a ring encircling the ...The multifunctional cytokine TGF-β is a dimeric protein produced within a latent complex (L-TGF-β). Latency is maintained by disulfide linked homodimeric prodomains forming a ring encircling the non-covalently bound mature TGF-β homodimer. This configuration sterically inhibits mature TGF-β from binding to its receptors. For TGF-β to be activated and bind to its receptors it must either be released, or if not released, overcome steric hinderance within the latent complex. Integrin binding to L-TGF-β results in activation with or without release of TGF-β by deforming the ring through different yet incompletely understood mechanisms. The domain architecture of L-TGF-β, which is not clearly defined, is a gap in mechanistic understanding of L-TGF-β activation. Here we fill this critical gap-in-knowledge by definitive experimental evidence demonstrating a domain-swapped architecture of L-TGF-β.
External linksNat Commun / PubMed:41290649 / PubMed Central
MethodsEM (single particle)
Resolution7.22 Å
Structure data

EMDB-47130: cryoEM map of avb8/mutant-L-TGF-b1/GARP/28G11
Method: EM (single particle) / Resolution: 7.22 Å

Source
  • Homo sapiens (human)

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