AI Article Synopsis
- The study used NMR spectroscopy to investigate the extracellular domain structure of BMP receptor IA both in its unbound state and when bound to BMP-2.
- While most of the secondary structure remains similar in both states, significant changes occur in the beta4beta5 loop, which is crucial for BMP-2 binding.
- The interactions involve conformational changes in both BMP-2 and BMPR-IA, indicating an induced fit mechanism that allows for a flexible and varied ligand-receptor interaction within the BMP protein superfamily.
Article Abstract
The structure of the extracellular domain of BMP receptor IA was determined in solution by NMR spectroscopy and compared to its structure when bound to its ligand BMP-2. While most parts of the secondary structure are highly conserved between the bound and unbound forms, large conformational rearrangements can be observed in the beta4beta5 loop of BMPR-IA, which is in contact with BMP-2 and harbors the main binding determinants for the BMPR-IA-BMP-2 interaction. In its unbound form, helix alpha1 in BMPR-IA, which is in the center of the binding epitope for BMP-2, is missing. Since BMP-2 also shows conformational changes in the type I receptor epitope upon binding to BMPR-IA, both binding partners pass through an induced fit mechanism to adapt their binding interfaces to a given interaction surface. The inherent flexibility of both partners possibly explains the promiscuous ligand-receptor interaction observed in the BMP protein superfamily.
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