The solution structure of BMPR-IA reveals a local disorder-to-order transition 
upon BMP-2 binding

Klages, J; Kotzsch, A; Coles, M; Sebald, W; Nickel, J; Müller, T; Kessler, H

doi:10.1021/bi801059j

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The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding

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Coles, M
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Klages, J., Kotzsch, A., Coles, M., Sebald, W., Nickel, J., Müller, T., et al. (2008). The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding. Biochemistry, 47(46), 11930-11939. doi:10.1021/bi801059j.

Cite as: https://hdl.handle.net/21.11116/0000-000B-25AC-A

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.