Extended Data Fig. 6: Additional analysis of LIS1-bound dynein_MOTOR^MT-U structure.

(a) 2 LIS1-bound dynein_MOTOR^MT-U structure with domains colored as shown in Fig. 5 (left) and the same shown with the full-length LIS1 homodimer, with the N-terminal dimerization domain modeled. The LIS1 N-terminal dimer model was generated using a combination of AlphaFold prediction⁶⁹ and a previous crystal structure, 1UUJ⁸². The structure was manually adjusted in COOT. (b) View of LIS1 homodimer surface that contacts site^stalk (teal) and site^ring (cyan). Residues listed and indicated in different colors on the structure are those that make direct contact with dynein or LIS1. Residues with ‘*’ are those identified in a recent study to make contact with wild-type human dynein⁴¹. (c) Side-view of full-length LIS1 homodimer model with residues colored as in panel b. (d) Results of molecular dynamics simulation from Fig. 5g depicting change in interatomic distances in residues mediating contacts between LIS1 and dynein as a consequence of indicated mutations.