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bioRxiv · 10.1101/2024.09.27.615443

Latent-TGF-β has a domain swapped architecture

Jin, M.·Seed, R.·Shing, T.·Cheng, Y.·Nishimura, S.
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Abstract

The multifunctional cytokine TGF-{beta} is produced in a latent form (L-TGF-{beta}) where a RGD containing homodimeric prodomain forms a "ring" encircling mature TGF-{beta} shielding it from its receptors. Thus L-TGF-{beta} must be activated to function, a process driven by dynamic allostery resulting from integrin binding the L-TGF-{beta} RGD motif. Here we provide critical evidence that defines a domain-swapped architecture of L-TGF-{beta}, an essential component in the dynamic allostery mechanism of L-TGF-{beta} activation.

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Jin, M., Seed, R., Shing, T., Cheng, Y., Nishimura, S.. 2024-09-30. Latent-TGF-β has a domain swapped architecture. https://doi.org/10.1101/2024.09.27.615443

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