Fig. 4: Detailed BMP10:BMPRII interface interactions.

a BMP10:BMPRII binding interface in complex AC. BMP10 (in coral)-binding surface on BMPRII (purple) can be broadly divided into three regions. The central hydrophobic triad (Y67, W85 and F115), the β4 strand to the A-loop (green oval), the F3-loop and the region connecting the A-loop and the F3-loop (light blue circle and orange oval). b–f Detailed interactions between BMP10 and BMPRII, at the β4 strand and A-loop region in all complexes (b), at the F3-loop (c) and the regions connecting the A-loop and the F3-loop in complex AC (d), at BMPRII S107 region in complex BD (e) and AB (f). BMP10 is shown in coral sticks throughout b–f, whereas BMPRII is in grey for complex BD, in dark blue for complex AB, in yellow for complex DL, in magenta for complex CK, in cyan for complex BJ and in green for complex AI. In a–f red dashed lines denote H-bonds, with distance all between 2.7-3.7 Å if not labelled. Underlined residue numbers are those from BMP10, and residues numbers in normal text are those from BMPRII. g Buried interface area between BMP10 and BMPRII in binary and ternary receptor complexes. *Complex BD has much smaller buried surface area because some sidechains at the interface were deleted between the A-loop and F3-loop due to poor densities.