|
Figure 7.
Figure 7. A Model for LIS1/Ndel1 and Its Interacton with
DyneinTo reconcile the two-fold symmetry of LIS1 with that of
Ndel1, we postulated that Ndel1 forms an antiparallel coiled
coil. The α4 helices of N-LIS1 interact with Ndel1, and so does
the β propeller region. The two β propellers of LIS1 bind
dynein at distinct sites in the first AAA module and in the stem
(Tai et al., 2002). Because the dynein heavy chain that
contributes a sizable fraction of the stem is a dimer (Holzbaur
and Vallee, 1994), the overall assembly may be duplicated
(represented by the gray, dashed drawing).
|
