The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding.
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Klages J, Kotzsch A, Coles M, Sebald W, Nickel J, Muller T, Kessler H
The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding.
Biochemistry. 2008 Nov 18;47(46):11930-9. doi: 10.1021/bi801059j. Epub 2008 Oct 21.
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- 18937504 [ View in PubMed]
- 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.