Fig. 5: Conserved region 2 and type II site analysis.
From: Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms
a ActRIIb-binding residues (based on PDB:4FAO, ActRIIb in semi-transparent cartoon) are mapped onto BMP9 surface (grey), with those conserved across all BMPs in Fig. 3a coloured in red, those from conserved region 2 in blue, and other variable residues in yellow. b Type II binding surface of BMP9 (left) and BMP10 (right), showing as electrostatic surface (generated in PyMOL, red representing negatively charged and blue positively charged surface). ActRIIb is shown in orange, semi-transparent cartoon. c Residues from BMP9 conserved region 2 make three backbone β-sheet and one sidechain H-bond interactions with ENG (PDB:5HZW, ENG in green, BMP9 in cyan). BMP10 is overlaid onto BMP9 and shown in grey, with four conserved region 2 residues shown in blue spheres. Sidechains of other residues are omitted for clarity. d Sequence alignment of human BMP10 prodomain (hBMP10_pro) with mouse BMP9 prodomain (mBMP9_pro) and human BMP9 prodomain (hBMP9_pro). Residues at the BMP9-binding surface are highlighted in yellow and those that make direct interactions with BMP9 GF-domain are marked with *. Residues that make main chain interactions are also marked with ^. Only the prodomain regions that interact with BMP9 GF-domain are shown, and full-length alignment of hBMP9_pro and hBMP10_pro can be found in Supplementary Fig. 5. e Residues in conserved region 2 of BMP9 make four backbone H-bond β-sheet interactions with prodomain (PDB:4YCG; prodomain in orange, BMP9 in cyan. BMP10 is overlaid on BMP9 and shown in grey. Four conserved BMP10 residues are in blue spheres).
