10.7554/eLife.18675.013Figure 5—figure supplement 2. Comparison with other Rab:effector structures.
The main interacting helix (α3) in the structure of Rab10:Mical-cL adopts a very similar relative position as the main interacting helices of the effector proteins in the structures of Rab3:Rabphilin-3a (pdb 1ZBD) (Ostermeier and Brunger, 1999), Rab27:Slp2a (pdb 3BC1) (Chavas et al., 2008) and Rab27:Slac2-a (pdb 2ZET) (Kukimoto-Niino et al., 2008). Furthermore, a basic Arg and an acidic Asp are conserved in all structures (in Rab3:Rabphilin-3a, only the Arg is conserved) and contact the residues corresponding to Asp45 and Gln61 in Rab10.
DOI: http://dx.doi.org/10.7554/eLife.18675.013