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2H64

Crystal structure of a ternary ligand-receptor complex of BMP-2

2H64 の概要
エントリーDOI10.2210/pdb2h64/pdb
関連するPDBエントリー1REU 2H62
分子名称Bone morphogenetic protein 2, Bone morphogenetic protein receptor type IA, Acvr2b protein, ... (4 entities in total)
機能のキーワードtgf-beta superfamily, ligand-receptor complex, hormone-growth factor complex, hormone/growth factor
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3
化学式量合計38789.55
構造登録者
Mueller, T.D.,Sebald, W.,Weber, D. (登録日: 2006-05-30, 公開日: 2007-04-10, 最終更新日: 2024-10-30)
主引用文献Weber, D.,Kotzsch, A.,Nickel, J.,Harth, S.,Seher, A.,Mueller, U.,Sebald, W.,Mueller, T.D.
A silent H-bond can be mutationally activated for high-affinity interaction of BMP-2 and activin type IIB receptor.
Bmc Struct.Biol., 7:6-6, 2007
Cited by
PubMed Abstract: Bone morphogenetic proteins (BMPs) are key regulators in the embryonic development and postnatal tissue homeostasis in all animals. Loss of function or dysregulation of BMPs results in severe diseases or even lethality. Like transforming growth factors beta (TGF-betas), activins, growth and differentiation factors (GDFs) and other members of the TGF-beta superfamily, BMPs signal by assembling two types of serine/threonine-kinase receptor chains to form a hetero-oligomeric ligand-receptor complex. BMP ligand receptor interaction is highly promiscuous, i.e. BMPs bind more than one receptor of each subtype, and a receptor bind various ligands. The activin type II receptors are of particular interest, since they bind a large number of diverse ligands. In addition they act as high-affinity receptors for activins but are also low-affinity receptors for BMPs. ActR-II and ActR-IIB therefore represent an interesting example how affinity and specificity might be generated in a promiscuous background.
PubMed: 17295905
DOI: 10.1186/1472-6807-7-6
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.92 Å)
構造検証レポート
Validation report summary of 2h64
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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