The multifunctional cytokine TGF-b is produced in a latent form (L-TGF-b) where a RGD containing homodimeric prodomain forms a "ring" encircling mature TGF-b, shielding it from its receptors. Thus L-TGF-b must be activated to function, a process driven by dynamic allostery resulting from integrin binding the L-TGF-b RGD motif. Here we provide critical evidence that defines a domain-swapped architecture of L-TGF-b, an essential component in the dynamic allostery mechanism of L-TGF-b activation.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11581116 | PMC |
| http://dx.doi.org/10.21203/rs.3.rs-5154292/v1 | DOI Listing |
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