1LXI

Refinement of BMP7 crystal structure

1LXI の概要

• エントリーDOI: 10.2210/pdb1lxi/pdb
• 関連するPDBエントリー: 1BMP
• 分子名称: BONE MORPHOGENETIC PROTEIN 7, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: cystine-knot growth factor, hormone-growth factor complex, hormone/growth factor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P18075
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15920.94

構造登録者

Greenwald, J.,Groppe, J.,Kwiatkowski, W.,Choe, S. (登録日: 2002-06-05, 公開日: 2003-04-01, 最終更新日: 2024-10-30)

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

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: 12667445
DOI: 10.1016/S1097-2765(03)00094-7

実験手法

X-RAY DIFFRACTION (2 Å)