10.7554/eLife.18675.010Figure 4. Structure of the Rab binding domain of Mical-3.
Mical-3 folds into three α-helices, the central α-helix 2 and α-helices 1 and 3 folding back on the central helix. The dimer observed in the asymmetric unit is formed mostly by hydrophobic interactions involving the same hydrophobic patches in both monomers, and α-helices 2 and 3 from each monomer form a central 4-stranded coiled-coil.
DOI: http://dx.doi.org/10.7554/eLife.18675.010