Figure 5.

Structure of the MORF9^86–186 MORF domain and its dimerization in relation to MORF1. (A) Overview of the MORF9^86–186 structure. A central MORF9^86–186 molecule (teal) forms a tight nearly symmetrical head-to-head dimer via a hydrophobic interaction surface with a second MORF9^86–186 molecule (yellow). (B) Close-up view of the main hydrophobic protein–protein interface of MORF9^86–186 shown in (A). (C) Superimposition of the MORF1^79–190 (marine blue and orange) and MORF9^86–186 (teal and yellow) dimers. Loops are omitted for clarity. The second MORF9^86–186 molecule (yellow) is rotated by an angle of ∼40° with respect to the respective MORF1^79–190 moiety (orange) as indicated for β-strand 4. (D) Close-up view of a peripheral MORF9^86–186 interface of the dimer shown in (A). (E and F) Comparison of the hydrophobic dimerization interfaces of MORF1^79–190 and MORF9^86–186. The selection of interacting residues is limited to positional or sequence identities shared by MORF1 and MORF9. Interacting residues are shown as sticks and colored by atom type. Carbon – as for the respective molecule; nitrogen – blue; oxygen – red; sulfur – yellow. Water oxygens are shown as green spheres. Dashed lines between atoms represent hydrogen bonds. Rotation symbols indicate views relative to Figure 2A.