1LXI
Refinement of BMP7 crystal structure
Summary for 1LXI
Entry DOI | 10.2210/pdb1lxi/pdb |
Related | 1BMP |
Descriptor | BONE MORPHOGENETIC PROTEIN 7, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | cystine-knot growth factor, hormone-growth factor complex, hormone/growth factor |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: P18075 |
Total number of polymer chains | 1 |
Total formula weight | 15920.94 |
Authors | Greenwald, J.,Groppe, J.,Kwiatkowski, W.,Choe, S. (deposition date: 2002-06-05, release date: 2003-04-01, Last modification date: 2024-10-30) |
Primary citation | Greenwald, J.,Groppe, J.,Gray, P.,Wiater, E.,Kwiatkowski, W.,Vale, W.,Choe, S. The BMP7/ActRII Extracellular Domain Complex Provides New Insights into the Cooperative Nature of Receptor Assembly Mol.Cell, 11:605-617, 2003 Cited by PubMed Abstract: Activins and bone morphogenetic proteins (BMPs) elicit diverse biological responses by signaling through two pairs of structurally related type I and type II receptors. Here we report the crystal structure of BMP7 in complex with the extracellular domain (ECD) of the activin type II receptor. Our structure produces a compelling four-receptor model, revealing that the types I and II receptor ECDs make no direct contacts. Nevertheless, we find that truncated receptors lacking their cytoplasmic domain retain the ability to cooperatively assemble in the cell membrane. Also, the affinity of BMP7 for its low-affinity type I receptor ECD increases 5-fold in the presence of its type II receptor ECD. Taken together, our results provide a view of the ligand-mediated cooperative assembly of BMP and activin receptors that does not rely on receptor-receptor contacts. PubMed: 12667445DOI: 10.1016/S1097-2765(03)00094-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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