1ES7

COMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINS

Summary for 1ES7

• Entry DOI: 10.2210/pdb1es7/pdb
• Related: 3BMP
• Descriptor: BONE MORPHOGENETIC PROTEIN-2, BONE MORPHOGENETIC PROTEIN RECEPTOR IA (3 entities in total)
• Functional Keywords: protein-protein complex, three finger toxin fold, receptor-ligand complex, cytokine receptor, tgf beta superfamily, cytokine
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P12643; Membrane; Single-pass type I membrane protein: P36894
• Total number of polymer chains: 4
• Total formula weight: 46056.74

Authors

Kirsch, T.,Sebald, W.,Dreyer, M.K. (deposition date: 2000-04-07, release date: 2000-10-07, Last modification date: 2024-10-30)

Primary citation

Kirsch, T.,Sebald, W.,Dreyer, M.K.
Crystal structure of the BMP-2-BRIA ectodomain complex.
Nat.Struct.Biol., 7:492-496, 2000

PubMed Abstract: Bone morphogenetic proteins (BMPs) belong to the large transforming growth factor-beta (TGF-beta) superfamily of multifunctional cytokines. BMP-2 can induce ectopic bone and cartilage formation in adult vertebrates and is involved in central steps in early embryonal development in animals. Signaling by these cytokines requires binding of two types of transmembrane serine/threonine receptor kinase chains classified as type I and type II. Here we report the crystal structure of human dimeric BMP-2 in complex with two high affinity BMP receptor IA extracellular domains (BRIAec). The receptor chains bind to the 'wrist' epitopes of the BMP-2 dimer and contact both BMP-2 monomers. No contacts exist between the receptor domains. The model reveals the structural basis for discrimination between type I and type II receptors and the variability of receptor-ligand interactions that is seen in BMP-TGF-beta systems.

PubMed: 10881198
DOI: 10.1038/75903

Experimental method

X-RAY DIFFRACTION (2.9 Å)