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3QB4

Crystal structure of a TGF-beta ligand-receptor complex

Summary for 3QB4
Entry DOI10.2210/pdb3qb4/pdb
Related1REW 1WAQ 2K3G 3EVS 3NH7
DescriptorGrowth/differentiation factor 5, Bone morphogenetic protein receptor type-1A (3 entities in total)
Functional Keywordscystine-knot, ligand-receptor complex, protein, membrane/extracellular, cytokine-transferase receptor complex, cytokine/transferase receptor
Biological sourceHomo sapiens (human)
More
Cellular locationSecreted : P43026
Membrane; Single-pass type I membrane protein: P36894
Total number of polymer chains4
Total formula weight55987.63
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 citationKlammert, 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: 26385096
DOI: 10.1186/s12915-015-0183-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.28 Å)
Structure validation

226707

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