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. 2020 Feb 25;11:1038. doi: 10.1038/s41467-020-14842-8

Fig. 7. A model for the directional bias for the applied forces and movement direction of dynein.

Fig. 7

a MTBD of dynein makes an initial attachment via a weak-binding interface (H1 and H6). b Backward force or diffusive search in the forward direction tilts MTBD, rendering H3 proximate to the binding site of β-tubulin (indicated by an arrow). c MT binding by MTBD via a strong-binding interface (H1, H3, and H6) induces the sliding of CC1, which would transmit the signal toward the ATPase domain to facilitate ATP hydrolysis and the release of Pi.