1LX5
Crystal Structure of the BMP7/ActRII Extracellular Domain Complex
1LX5 の概要
エントリーDOI | 10.2210/pdb1lx5/pdb |
関連するPDBエントリー | 1LXI |
分子名称 | bone morphogenetic protein 7, Activin Type II Receptor, alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-4)][alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
機能のキーワード | ligand-receptor complex, growth factor-growth factor receptor complex, growth factor/growth factor receptor |
由来する生物種 | Homo sapiens (human) 詳細 |
細胞内の位置 | Secreted: P18075 Membrane; Single-pass type I membrane protein: P27038 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 29234.55 |
構造登録者 | Greenwald, J.,Groppe, J.,Kwiatkowski, W.,Choe, S. (登録日: 2002-06-04, 公開日: 2003-04-01, 最終更新日: 2024-10-16) |
主引用文献 | Greenwald, J.,Groppe, J.,Gray, P.,Wiater, E.,Kwiatkowski, W.,Vale, W.,Choe, S. The BMP7/ActRII Extracellular Domain Complex Provides New Insights into the Cooperative Nature of Receptor Assembly Mol.Cell, 11:605-617, 2003 Cited by PubMed Abstract: Activins and bone morphogenetic proteins (BMPs) elicit diverse biological responses by signaling through two pairs of structurally related type I and type II receptors. Here we report the crystal structure of BMP7 in complex with the extracellular domain (ECD) of the activin type II receptor. Our structure produces a compelling four-receptor model, revealing that the types I and II receptor ECDs make no direct contacts. Nevertheless, we find that truncated receptors lacking their cytoplasmic domain retain the ability to cooperatively assemble in the cell membrane. Also, the affinity of BMP7 for its low-affinity type I receptor ECD increases 5-fold in the presence of its type II receptor ECD. Taken together, our results provide a view of the ligand-mediated cooperative assembly of BMP and activin receptors that does not rely on receptor-receptor contacts. PubMed: 12667445DOI: 10.1016/S1097-2765(03)00094-7 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.3 Å) |
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