2B0U
The Structure of the Follistatin:Activin Complex
2B0U の概要
| エントリーDOI | 10.2210/pdb2b0u/pdb |
| 分子名称 | Inhibin beta A chain, Follistatin, IRIDIUM (III) ION, ... (6 entities in total) |
| 機能のキーワード | activin, follistatin, tgf-beta, morphogen, inhibin, signaling protein |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Secreted: P08476 P19883 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 90655.58 |
| 構造登録者 | Thompson, T.B.,Lerch, T.F.,Cook, R.W.,Woodruff, T.K.,Jardetzky, T.S. (登録日: 2005-09-14, 公開日: 2005-10-11, 最終更新日: 2024-10-30) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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