Fig. 1: Structure of the Chi dynein–Lis1 complex.
From: Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedge
a, Cartoons of the domain organization of dynein and Lis1. Major elements mentioned in the text are labeled. MTBD, microtubule binding domain. b, Schematic of dynein activation. Activation of dynein requires the relief of its autoinhibited conformation (Phi) and the formation of an active complex containing the dynactin complex and an activating adapter. Although Lis1 is known to be involved in this process, how it is involved is unknown. c, Cryo-EM map of the Chi dynein–Lis1 complex (non-symmetry expanded), shown in two orientations. The different Lis1 β-propellers that bind to previously identified sites on dynein are labeled. d, Model of the Chi dynein–Lis1 complex, shown in the same two orientations as in the map in c.
