We have officially solved our fourth follistatin 288 structure in complex with an activin family ligand, this time with activin B.
Using our novel structure, computational analysis, and molecular dynamics simulations, we interrogate the antagonist's ligand specificity.
www.jbc.org/article/S002...
jbc.org
The crystal structure of the activin B:Fst288 complex and computational insights into the broad antagonistic activity and specificity of follistatin
Members of the transforming growth factor-β (TGF-β) family regulate essential biological processes, and their activity is tightly controlled by extracellular antagonists like follistatin 288 (Fst288). While Fst288 potently inhibits several ligands, including activins A and B, GDF8, and GDF11, the structural basis for its interaction with activin B (ActB) has remained largely uncharacterized. This lack of data has limited our understanding of how Fst288 achieves such broad inhibitory activity while maintaining ligand-specific selectivity.
