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. Author manuscript; available in PMC: 2011 Apr 16.
Published in final edited form as: Cell. 2010 Apr 16;141(2):304–314. doi: 10.1016/j.cell.2010.02.035

Fig. 7. Diagrammatic representation of dynein-LIS1-NudE interactions and functional consequences.

Fig. 7

(A) Bar diagram of NudE shows coiled-coil and unstructured C-terminal domains, and known LIS1 and dynein binding regions (see text for details). (B) Proposed assembly intermediates in dynein-NudE-LIS1 complex. Known binding of NudE to dynein intermediate and light chains (Stehman et al., 2007) predicts association of NudE C-terminus with base of the dynein molecule and protruding coiled-coil domain as shown. The calculated distance between this site and the known LIS1 binding site in the middle of the NudE coiled-coil α-helical tail (Derewenda et al., 2007) is proposed here to be sufficient to allow NudE to position LIS1 near the dynein motor domains. LIS1 is shown unbound to the dynein motor domain as we observe under most conditions, but is proposed to bind specifically in the ADP-VO4 prepowerstroke state (Fig. 2).