1ES7

COMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINS

1ES7 の概要

• エントリーDOI: 10.2210/pdb1es7/pdb
• 関連するPDBエントリー: 3BMP
• 分子名称: BONE MORPHOGENETIC PROTEIN-2, BONE MORPHOGENETIC PROTEIN RECEPTOR IA (3 entities in total)
• 機能のキーワード: protein-protein complex, three finger toxin fold, receptor-ligand complex, cytokine receptor, tgf beta superfamily, cytokine
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted: P12643; Membrane; Single-pass type I membrane protein: P36894
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 46056.74

構造登録者

Kirsch, T.,Sebald, W.,Dreyer, M.K. (登録日: 2000-04-07, 公開日: 2000-10-07, 最終更新日: 2024-10-30)

主引用文献

Kirsch, T.,Sebald, W.,Dreyer, M.K.
Crystal structure of the BMP-2-BRIA ectodomain complex.
Nat.Struct.Biol., 7:492-496, 2000

PubMed Abstract: Bone morphogenetic proteins (BMPs) belong to the large transforming growth factor-beta (TGF-beta) superfamily of multifunctional cytokines. BMP-2 can induce ectopic bone and cartilage formation in adult vertebrates and is involved in central steps in early embryonal development in animals. Signaling by these cytokines requires binding of two types of transmembrane serine/threonine receptor kinase chains classified as type I and type II. Here we report the crystal structure of human dimeric BMP-2 in complex with two high affinity BMP receptor IA extracellular domains (BRIAec). The receptor chains bind to the 'wrist' epitopes of the BMP-2 dimer and contact both BMP-2 monomers. No contacts exist between the receptor domains. The model reveals the structural basis for discrimination between type I and type II receptors and the variability of receptor-ligand interactions that is seen in BMP-TGF-beta systems.

PubMed: 10881198
DOI: 10.1038/75903

実験手法

X-RAY DIFFRACTION (2.9 Å)