Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP‐2

@article{Kirsch2000IsolationOR,
  title={Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP‐2},
  author={Thomas A Kirsch and Joachim Nickel and Walter Sebald},
  journal={FEBS Letters},
  year={2000},
  volume={468}
}

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.

Molecular recognition of BMP-2 and BMP receptor IA

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

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.

Type I receptor binding of bone morphogenetic protein 6 is dependent on N‐glycosylation of the ligand

Bone morphogenetic proteins (BMPs), together with transforming growth factor (TGF)‐β and activins/inhibins, constitute the TGF‐β superfamily of ligands, and N‐glycosylation at Asn73 of BMP‐6 in the wrist epitope is crucial for recognition by the activin receptor type I.

The Crystal Structure of the BMP-2: BMPR-IA Complex and the Generation of BMP-2 Antagonists

The identification and characterization of the two receptor binding epitopes in BMP-2 provide new insight into the primary steps of B MP-receptor activation and are transferable to other TGF-&bgr; receptor systems.

BMP-3 and BMP-6 structures illuminate the nature of binding specificity with receptors.

It is illustrated how a single amino acid can regulate the specificity of ligand-receptor binding and potentially alter biological signaling and function in vivo.

A silent H-bond can be mutationally activated for high-affinity interaction of BMP-2 and activin type IIB receptor

The structure-/function studies presented here revealed a new mechanism, in which the energy contribution of a conserved H-bond is modulated by surrounding intramolecular interactions to achieve a switch between low- and high-affinity binding.

A Selection Fit Mechanism in BMP Receptor IA as a Possible Source for BMP Ligand-Receptor Promiscuity

The functional and structural analysis of the BMPR-IA binding antibody AbD1556 mimicking the BMP-2 binding epitope may pave the way for the design of low-molecular weight synthetic receptor binders/inhibitors.
...

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