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. Author manuscript; available in PMC: 2019 Aug 6.
Published in final edited form as: Nature. 2019 Feb 6;566(7744):407–410. doi: 10.1038/s41586-019-0914-z

Extended Data Figure 2 ∣. Engineering the directionality of dynein motility.

Extended Data Figure 2 ∣

Schematic diagram of the helices (CC1 and CC2) at the stalk of yeast cytoplasmic dynein shows the heptad repeat hydrophobic contacts (black lines) in the core of the coiled-coil when dynein is at low MT affinity (β) state. Conserved proline residues at the base of Dyn’s stalk are highlighted with magenta arrows. 3 heptads deleted from the stalk of Dyn−3hep are highlighted with green in Dyn. 3 and 7 heptad repeats inserted to Dyn+3hep, Dyn+7hep and DynRK+7hep are highlighted in red. The inserted sequences were taken from the Drosophila melanogaster cytoplasmic dynein12. Point mutations inserted to DynRK and DynRK+7hep are highlighted in cyan.