3QB4

Crystal structure of a TGF-beta ligand-receptor complex

3QB4 の概要

• エントリーDOI: 10.2210/pdb3qb4/pdb
• 関連するPDBエントリー: 1REW 1WAQ 2K3G 3EVS 3NH7
• 分子名称: Growth/differentiation factor 5, Bone morphogenetic protein receptor type-1A (3 entities in total)
• 機能のキーワード: cystine-knot, ligand-receptor complex, protein, membrane/extracellular, cytokine-transferase receptor complex, cytokine/transferase receptor
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted : P43026; 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: 55987.63

構造登録者

Mueller, T.D.,Nickel, J.,Sebald, W. (登録日: 2011-01-12, 公開日: 2012-03-14, 最終更新日: 2024-11-06)

主引用文献

Klammert, U.,Mueller, T.D.,Hellmann, T.V.,Wuerzler, K.K.,Kotzsch, A.,Schliermann, A.,Schmitz, W.,Kuebler, A.C.,Sebald, W.,Nickel, J.
GDF-5 can act as a context-dependent BMP-2 antagonist.
Bmc Biol., 13:77-77, 2015

PubMed Abstract: Bone morphogenetic protein (BMP)-2 and growth and differentiation factor (GDF)-5 are two related transforming growth factor (TGF)-β family members with important functions in embryonic development and tissue homeostasis. BMP-2 is best known for its osteoinductive properties whereas GDF-5-as evident from its alternative name, cartilage derived morphogenetic protein 1-plays an important role in the formation of cartilage. In spite of these differences both factors signal by binding to the same subset of BMP receptors, raising the question how these different functionalities are generated. The largest difference in receptor binding is observed in the interaction with the type I receptor BMPR-IA. GDF-5, in contrast to BMP-2, shows preferential binding to the isoform BMPR-IB, which is abrogated by a single amino acid (A57R) substitution. The resulting variant, GDF-5 R57A, represents a "BMP-2 mimic" with respect to BMP receptor binding. In this study we thus wanted to analyze whether the two growth factors can induce distinct signals via an identically composed receptor.

PubMed: 26385096
DOI: 10.1186/s12915-015-0183-8

実験手法

X-RAY DIFFRACTION (2.28 Å)