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The Mode of Bone Morphogenetic Protein (BMP) Receptor Oligomerization Determines Different BMP-2 Signaling Pathways*
It is shown that the ability of kinase-deficient BRII receptor mutants to inhibit BMP signaling depends on their ability to form heteromeric complexes with BRI, and a BRII mutant that is incapable in forming preassembled receptor complexes but recruits into a BMP-induced receptor complex does not interfere with the Smad pathway but does inhibit the induction of alkaline phosphatase as well as p38 phosphorylation.
Human bone morphogenetic protein 2 contains a heparin-binding site which modifies its biological activity.
The results identify the basic N-terminal domains of dimeric BMP-2 as heparin-binding sites that are not obligatory for receptor activation but modulate its biological activity.
Crystal structure of the BMP-2–BRIA ectodomain complex
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-β systems.
Crossveinless 2 is an essential positive feedback regulator of Bmp signaling during zebrafish gastrulation
It is shown that zebrafish cvl2 is required in a positive feedback loop to promote Bmp signaling during embryonic dorsoventral patterning, identifying Cvl2 as an essential pro-Bmp factor during zebra fish embryogenesis, emphasizing the functional diversity of Bmp binding CR-domain proteins.
Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction
Mutational and interaction analyses indicate that the large hydrophobic core of the interface of BMP-2 (wrist epitope) with the type I receptor does not provide a hydrophilic hot spot for binding, and main chain amide and carbonyl groups that are completely buried in the contact region represent major binding determinants.
BMP‐2 antagonists emerge from alterations in the low‐affinity binding epitope for receptor BMPR‐II
These findings provide a framework for the molecular description of receptor recognition and activation in the BMP/TGF‐β superfamily.
Molecular recognition of BMP-2 and BMP receptor IA
- S. Keller, J. Nickel, Jin-li Zhang, W. Sebald, T. Mueller
- Biology, ChemistryNature Structural &Molecular Biology
- 4 April 2004
Bone morphogenetic protein-2 (BMP-2) and other members of the TGF-β superfamily regulate the development, maintenance and regeneration of tissues and organs. Binding epitopes for these extracellular…
Structure, binding, and antagonists in the IL-4/IL-13 receptor system.
A single residue of GDF-5 defines binding specificity to BMP receptor IB.