Nature CommunicationsBiophysicsPeer-reviewed journal article
Latent-TGF-β has a domain swapped architecture
Mingliang JiniD, Robert SeediD, Tiffany Shing, Li WangiD, Junrui LiiD, Yifan ChengiD, Stephen L. NishimuraiD
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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