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Figure 2.
Figure 2. L5 and MT Binding Region in NOD Show Unique
Conformation Compared to Other Kinesins
(A) Comparison of
L5 in different kinesin families (gray) after P loop
superposition. The N-terminal half of L5 in NOD (blue) packs
against α3.
(B) Detailed view of L5 in NOD (blue) compared
to L5 in kinesin-5 (orange) bound to monastrol (Mon). The pocket
formed by P101 and P102 on L5 and L180, H181, and L184 on α3 is
shown.
(C) NOD•ADP (blue) was superposed with KHC•ADP
(gold) and oriented to show the β5-L8 lobe.
(D–F) NOD's
“Sw2 cluster” (blue) is compared to the “ADP-like”
conformation in kinesin-1 ([D], 1bg2, magenta), the
“ATP-like” conformation in kinesin-1 ([E], 1mkj, gold), and
KIF2C ([F], 1v8j, red). View is from the MT binding surface.
Clockwise rotation of NOD's α4 relative to kinesin-1's α4 is
highlighted in (D) and (E).
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