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Figure 1.
Figure 1: The tubulin-colchicine:RB3-SLD complex. a, The
complex includes two tubulin   heterodimers,
with colchicine bound to subunits
at the interface with .
The RB3-SLD connecting region (residues 29-45) is from
tubulin-podophyllotoxin:RB3-SLD, where it is clearest
(podophyllotoxin is a competitive inhibitor of colchicine
binding to tubulin23). b, The hairpin
(orange) in the N-terminal domain of RB3-SLD caps the T2R
complex, extending the sheet
(yellow) of the intermediate domain in the 1
subunit. The extensive overlap with a protofilament (+ )-end
subunit15,
preventing the addition of the T2R complex to a microtubule, is
illustrated. c, Interactions of RB3-SLD residues with tubulin
(except for the least-well-defined RB3-SLD connecting region and
for the extension of the tubulin intermediate domain -sheet)
represented by yellow connecting areas. Red bars, residues of
the -helix
pointing towards tubulin. Dashed lines, main-chain hydrogen
bonds in the extension of the intermediate domain -sheet.
Within the internal repeat (grey), identical residues are
connected in blue (thick blue, side-chain pointing towards
tubulin). Asterisks indicate positions of stathmin
phosphorylation sites.
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