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Extra info for Bone morphogenic protein
Fajardo, R. , Manoharan, R. , Pearsall, R. , Davies, M. , Monnell, T. , et al. (2010). Treatment with a soluble receptor for activin improves bone mass and structure in the axial and appendicular skeleton of female cynomolgus macaques (Macaca fascicularis). Bone, 46(1), 64–71. 018. 46 Thomas D. , Wang, S. , & Bonadio, J. (1997). Genes coding for mouse activin beta C and beta E are closely linked and exhibit a liver-specific expression pattern in adult tissues. Biochemical and Biophysical Research Communications, 231(3), 655–661.
2004). Compared with the rigid BMP/GDF ligands, the extracellular domains of the BMP receptors seem to be more flexible. g. , 2007). The concave side of the three-stranded β-sheet comprising the strands β3, β4, and β6, however, which contributes most to the ligand– receptor interface, is structurally almost identical in all three type II receptors independent on whether the structures were determined for their bound or unbound conformation suggesting that this interface element is preformed. Nevertheless, as some residues present in the flexible loops were identified to confer ligand–type II receptor specificity, flexibility of these elements might thus be important to implement the required degree of adaptability and specificity (Yeh, Falcon, Garces, Lee, & Lee, 2012).
The high adaptability of this interface is also evident Mechanisms of BMP–Receptor Interaction and Activation 31 from the interaction of BMPs and GDFs (as well in part also for Activins) with a plethora of structurally highly variable set of antagonists and modulator proteins. , 2008), the data clearly show that the BMP and Activin antagonists do neither share any structural similarity among each other nor with the receptors of the TGFβ superfamily (Fig. 6A–D). However, despite this structural dissimilarity, all modulator proteins bind to the same epitopes also recognized by the TGFβ type I and type II receptors strongly indicating that binding to a common epitope does not require structural mimicry.