2B0U
The Structure of the Follistatin:Activin Complex
Summary for 2B0U
| Entry DOI | 10.2210/pdb2b0u/pdb |
| Descriptor | Inhibin beta A chain, Follistatin, IRIDIUM (III) ION, ... (6 entities in total) |
| Functional Keywords | activin, follistatin, tgf-beta, morphogen, inhibin, signaling protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Secreted: P08476 P19883 |
| Total number of polymer chains | 4 |
| Total formula weight | 90655.58 |
| Authors | Thompson, T.B.,Lerch, T.F.,Cook, R.W.,Woodruff, T.K.,Jardetzky, T.S. (deposition date: 2005-09-14, release date: 2005-10-11, Last modification date: 2024-10-30) |
| Primary citation | Thompson, T.B.,Lerch, T.F.,Cook, R.W.,Woodruff, T.K.,Jardetzky, T.S. The Structure of the Follistatin:Activin Complex Reveals Antagonism of Both Type I and Type II Receptor Binding. Dev.Cell, 9:535-543, 2005 Cited by PubMed Abstract: TGF-beta ligands stimulate diverse cellular differentiation and growth responses by signaling through type I and II receptors. Ligand antagonists, such as follistatin, block signaling and are essential regulators of physiological responses. Here we report the structure of activin A, a TGF-beta ligand, bound to the high-affinity antagonist follistatin. Two follistatin molecules encircle activin, neutralizing the ligand by burying one-third of its residues and its receptor binding sites. Previous studies have suggested that type I receptor binding would not be blocked by follistatin, but the crystal structure reveals that the follistatin N-terminal domain has an unexpected fold that mimics a universal type I receptor motif and occupies this receptor binding site. The formation of follistatin:BMP:type I receptor complexes can be explained by the stoichiometric and geometric arrangement of the activin:follistatin complex. The mode of ligand binding by follistatin has important implications for its ability to neutralize homo- and heterodimeric ligands of this growth factor family. PubMed: 16198295DOI: 10.1016/j.devcel.2005.09.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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