2H62

Crystal structure of a ternary ligand-receptor complex of BMP-2

Summary for 2H62

• Entry DOI: 10.2210/pdb2h62/pdb
• Related: 1REU 2H64
• Descriptor: Bone morphogenetic protein 2, Bone morphogenetic protein receptor type IA, Acvr2b protein, ... (4 entities in total)
• Functional Keywords: tgf-beta superfamily, ligand-receptor complex, hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P36894; Membrane; Single-pass type I membrane protein: Q3KQI1
• Total number of polymer chains: 4
• Total formula weight: 51599.28

Authors

Mueller, T.D. (deposition date: 2006-05-30, release date: 2007-04-10, Last modification date: 2024-03-13)

Primary citation

Weber, D.,Kotzsch, A.,Nickel, J.,Harth, S.,Seher, A.,Mueller, U.,Sebald, W.,Mueller, T.D.
A silent H-bond can be mutationally activated for high-affinity interaction of BMP-2 and activin type IIB receptor.
Bmc Struct.Biol., 7:6-6, 2007

PubMed Abstract: Bone morphogenetic proteins (BMPs) are key regulators in the embryonic development and postnatal tissue homeostasis in all animals. Loss of function or dysregulation of BMPs results in severe diseases or even lethality. Like transforming growth factors beta (TGF-betas), activins, growth and differentiation factors (GDFs) and other members of the TGF-beta superfamily, BMPs signal by assembling two types of serine/threonine-kinase receptor chains to form a hetero-oligomeric ligand-receptor complex. BMP ligand receptor interaction is highly promiscuous, i.e. BMPs bind more than one receptor of each subtype, and a receptor bind various ligands. The activin type II receptors are of particular interest, since they bind a large number of diverse ligands. In addition they act as high-affinity receptors for activins but are also low-affinity receptors for BMPs. ActR-II and ActR-IIB therefore represent an interesting example how affinity and specificity might be generated in a promiscuous background.

PubMed: 17295905
DOI: 10.1186/1472-6807-7-6

Experimental method

X-RAY DIFFRACTION (1.85 Å)