Fig. 5: Structural comparison of the LRRK2:14-3-32 complex with active LRRK2.
From: 14-3-3 binding maintains the Parkinson’s associated kinase LRRK2 in an inactive state
a Side by side comparison of the LRRK2:14-3-32 complex (colored as in Fig. 1) and the active conformation of LRRK2 derived from a tetrameric structure (PDB: 8FO9, in gray), highlighting the Roc-COR domain rotation (indicated by an arrow). 14-3-3 proteins are omitted for clarity. b Superimposition of the COR domain from the LRRK2:14-3-32 complex (shown in coral) with the COR domain from the active LRRK2 (shown in gray). Alignments were performed by the COR-A domain (top and bottom left) and by the COR-B domain (bottom right), to illustrate the structural shifts and effects. c Binding affinity measurements of LRRK2 and 14−3-3γ in the presence of kinase inhibitors, as determined by MST in vitro. Data in (c) are mean ± SEM (n = 3 independent experiments), significance of difference was quantified using one-way Brown–Forsythe and Welch ANOVA test and reported with the exact p values in the source data file. Refer to Supplementary Fig. 17 for full binding curves.
