Journal
BIOCHEMISTRY
Volume 47, Issue 46, Pages 11930-11939Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi801059j
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- Deutsche Forschungsgemeinschaft (DFG) [MU1095/1-1, KE147/40-1]
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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 beta 4 beta 5 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 alpha 1 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 fiexibility of both partners possibly explains the promiscuous ligand-receptor interaction observed in the BMP protein superfamily.
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