Fig. 3: Overlap of the LRRK2:14-3-32 and LRRK2 homodimer interfaces.
From: 14-3-3 binding maintains the Parkinson’s associated kinase LRRK2 in an inactive state
a Structural comparison of the inactive LRRK2 homodimer (PDB: 7LHW, in gray, left) and the LRRK2:14-3-32 complex (colored as in Fig. 1), showing the overlapping interfaces mediated by the COR-B domain (right). Loops containing the S910 and S935 sites, flexible and unresolved in the dimer structure, are illustrated with dashed lines. b Surface representations of the COR-B domain. Left: residues involved in the LRRK2 dimer interface shaded in tan. Middle: residues involved in the LRRK2:14-3-32 interface shaded in gray. Right: Overlay of the two interfaces showing steric clash, suggesting mutual exclusivity between LRRK2 dimerization and 14-3-3 binding. c SEC-MALS chromatogram of the pre-formed LRRK2 dimer in the presence and absence of 14-3-3, indicating changes in molecular weight distribution.
