Fig. 1: Structure of the LRRK2:14-3-32 complex. | Nature Communications

Fig. 1: Structure of the LRRK2:14-3-32 complex.

From: 14-3-3 binding maintains the Parkinson’s associated kinase LRRK2 in an inactive state

Fig. 1

a Schematic representation of LRRK2 domain organization. Residues S910 and S935, which serve as 14-3-3 binding sites upon phosphorylation, are highlighted in red. b Cryo-EM density map at a resolution of 3.96 Å (left), with the corresponding structural model shown on the right. The model is colored according to the domain color code in (a) and shown in two different orientations for clarity.

Back to article page