1LX5

Crystal Structure of the BMP7/ActRII Extracellular Domain Complex

Summary for 1LX5

• Entry DOI: 10.2210/pdb1lx5/pdb
• Related: 1LXI
• Descriptor: bone morphogenetic protein 7, Activin Type II Receptor, alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-4)][alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: ligand-receptor complex, growth factor-growth factor receptor complex, growth factor/growth factor receptor
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P18075; Membrane; Single-pass type I membrane protein: P27038
• Total number of polymer chains: 2
• Total formula weight: 29234.55

Authors

Greenwald, J.,Groppe, J.,Kwiatkowski, W.,Choe, S. (deposition date: 2002-06-04, release date: 2003-04-01, Last modification date: 2024-10-16)

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

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: 12667445
DOI: 10.1016/S1097-2765(03)00094-7

Experimental method

X-RAY DIFFRACTION (3.3 Å)