2H64
Crystal structure of a ternary ligand-receptor complex of BMP-2
2H64 の概要
| エントリーDOI | 10.2210/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 | |
| 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: 17295905DOI: 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) |
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