3QB4
Crystal structure of a TGF-beta ligand-receptor complex
Summary for 3QB4
Entry DOI | 10.2210/pdb3qb4/pdb |
Related | 1REW 1WAQ 2K3G 3EVS 3NH7 |
Descriptor | Growth/differentiation factor 5, Bone morphogenetic protein receptor type-1A (3 entities in total) |
Functional Keywords | cystine-knot, ligand-receptor complex, protein, membrane/extracellular, cytokine-transferase receptor complex, cytokine/transferase receptor |
Biological source | Homo sapiens (human) More |
Cellular location | Secreted : P43026 Membrane; Single-pass type I membrane protein: P36894 |
Total number of polymer chains | 4 |
Total formula weight | 55987.63 |
Authors | Mueller, T.D.,Nickel, J.,Sebald, W. (deposition date: 2011-01-12, release date: 2012-03-14, Last modification date: 2023-09-13) |
Primary citation | 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 Cited by 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: 26385096DOI: 10.1186/s12915-015-0183-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.28 Å) |
Structure validation
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