Figure 4

The 3D homology model of the dimeric LRRK2 ARM domain. (a) The armadillo repeats of the two LRRK2 molecules establish a concave inner conformation to each monomer. In this model of the isolated ARM repeat domain, the sites capable of dimerization are lined with residues that establish a hydrophobic core. Shown are each of the modeled LRRK2 monomers (presented in blue and magenta ribbon) of the LRRK2 ARM region. Each structure bears a specific α-helical motif that is exposed on the molecule located near the C-terminus of the ARM repeat region. One such motif is highlighted in green. (b) When viewed from the side, the two monomers display a supercoiled dimeric-like formation that is typical of armadillo repeat containing proteins.