File:Ternary ligand-receptor complex of wildtype BMP-2.tiff

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Description Figure 1. Ternary ligand-receptor complex of wildtype BMP-2. Ribbon representation (stereo figure) of the crystal structure of wildtype BMP-2 (monomers in yellow and blue) bound to one receptor ectodomain of BMPR-IAECD (green) and ActR-IIBECD (red), (a) viewed from the side, (b) or from above. The unexpected stoichiometry 1:1:1 is due to crystal packing forces resulting in the loss of one BMPR-IAECD and one ActR-IIBECD molecule in the ternary complex.
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Source https://bmcstructbiol.biomedcentral.com/articles/10.1186/1472-6807-7-6 Weber, D., Kotzsch, A., Nickel, J. et al. A silent H-bond can be mutationally activated for high-affinity interaction of BMP-2 and activin type IIB receptor. BMC Struct Biol 7, 6 (2007). https://doi.org/10.1186/1472-6807-7-6
Author Weber, D., Kotzsch, A., Nickel, J. et al.
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Open Access This article is published under license to BioMed Central Ltd. This is an Open Access article is distributed under the terms of the Creative Commons Attribution License ( https://creativecommons.org/licenses/by/2.0 ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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current18:20, 18 December 2024Thumbnail for version as of 18:20, 18 December 20241,775 × 1,383 (1,014 KB)Rasbak (talk | contribs){{Information |description=Figure 1. Ternary ligand-receptor complex of wildtype BMP-2. Ribbon representation (stereo figure) of the crystal structure of wildtype BMP-2 (monomers in yellow and blue) bound to one receptor ectodomain of BMPR-IA<sub>ECD</sub> (green) and ActR-IIB<sub>ECD</sub> (red), (a) viewed from the side, (b) or from above. The unexpected stoichiometry 1:1:1 is due to crystal packing forces resulting in the loss of one BMPR-IA<sub>ECD</sub> and one ActR-IIB<sub>ECD</sub> mol...

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