Fig. 5: The Roc-COR-kinase interface.
From: Structure and regulation of full-length human leucine-rich repeat kinase 1
A Effect of mutations in this interface on Rab7A phosphorylation by recombinant LRRK1. Results presented are the quantification of multiple kinase assays from at least three independent protein preparations (see “Methods”, Supplementary Fig. 7D for representative membrane images and Supplementary Fig. 8D for complete membrane images, values are mean ± SEM, n = 6–36 independent assays from 9 independent protein preparations (WT, K1270M) or 3 independent protein preparations (all other mutants)). B Related to C–E, structure of LRRK1, with the position of the αC helix, COR-B DK and α1 helices and K746 indicated in the structure. C Cryo-EM density supporting the Roc/COR interface, additionally showing that the αC helix is positioned away from the interface in the inactive state. D Structural changes between the inactive-state cryo-EM model, and the active-state Alphafold model, highlighting a change in the position of K746 relative to the DK helix, and in the position of R1034. E Overlay of the DK helix/activation loop interface between the cryo-EM and Alphafold models, highlighting the movement of the DK helix towards the activation loop. In C the map shown is the composite cryo-EM density map. Source data is provided as a source data file.
