Extended Data Fig. 8: Binding characterization of Lis1 mutants and structural prediction of Lis1Δ300–304.
From: Nde1 promotes Lis1 binding to full-length autoinhibited human dynein 1
a, MP profiles show binding of Lis1 mutants to open dynein. Open dynein and Lis1 mutants were mixed at a 1:2 ratio and incubated for 2 min prior to measurements. b, MP profiles show binding of the Lis1AAA6 mutant to dynein with Nde1 at different incubation times. Dynein, Lis1AAA6, and Nde1 were mixed at 1:2:2 ratio (D: dynein only, DL: one dynein and one Lis1, DL2N: one dynein, two Lis1s, and one Nde1) and incubated for 2, 6, and 15 minutes before the measurements. c, The percentages of mass populations detected in b. d, Overlay of AlphaFold3-predicted Lis1Δ300-304 and WT Lis1 bound to PhiL dynein motor domains. Lis1Δ300-304 is shown in violet, while WT Lis1 is colored green and sky blue. Dynein motors domains are displayed in grey and white. The structure overlay indicates that deletion of residues 300–304 in Lis1 surface loop does not induce notable conformational change of the rigid elements of Lis1Δ300-304.
