3EVS
Crystal structure of the GDF-5:BMP receptor IB complex.
Summary for 3EVS
| Entry DOI | 10.2210/pdb3evs/pdb |
| Related | 1REW 1WAQ 2H62 2K3G 2QJB |
| Descriptor | Growth/differentiation factor 5, Bone morphogenetic protein receptor type-1B (3 entities in total) |
| Functional Keywords | ligand-receptor complex, cystin-knot ligand; three-finger toxn fold (receptor), cleavage on pair of basic residues, cytokine, disease mutation, dwarfism, glycoprotein, growth factor, secreted, atp-binding, kinase, magnesium, manganese, membrane, metal-binding, nucleotide-binding, receptor, serine/threonine-protein kinase, transferase, transmembrane, cytokine-transferase receptor complex, cytokine/transferase receptor |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Secreted: P43026 Membrane; Single-pass type I membrane protein: P36898 |
| Total number of polymer chains | 2 |
| Total formula weight | 26620.34 |
| Authors | Kotzsch, A.,Mueller, T.D. (deposition date: 2008-10-13, release date: 2009-03-10, Last modification date: 2024-10-16) |
| Primary citation | Kotzsch, A.,Nickel, J.,Seher, A.,Sebald, W.,Muller, T.D. Crystal structure analysis reveals a spring-loaded latch as molecular mechanism for GDF-5-type I receptor specificity. Embo J., 28:937-947, 2009 Cited by PubMed Abstract: Dysregulation of growth and differentiation factor 5 (GDF-5) signalling, a member of the TGF-beta superfamily, is strongly linked to skeletal malformation. GDF-5-mediated signal transduction involves both BMP type I receptors, BMPR-IA and BMPR-IB. However, mutations in either GDF-5 or BMPR-IB lead to similar phenotypes, indicating that in chondrogenesis GDF-5 signalling seems to be exclusively mediated through BMPR-IB. Here, we present structural insights into the GDF-5:BMPR-IB complex revealing how binding specificity for BMPR-IB is generated on a molecular level. In BMPR-IB, a loop within the ligand-binding epitope functions similar to a latch allowing high-affinity binding of GDF-5. In BMPR-IA, this latch is in a closed conformation leading to steric repulsion. The new structural data now provide also a molecular basis of how phenotypically relevant missense mutations in GDF-5 might impair receptor binding and activation. PubMed: 19229295DOI: 10.1038/emboj.2009.37 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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