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Space-filling
view of Tubulin:Stathmin like domain complex.
overview of the complex in which each tubulin is colored
differently. The α(β) subunits are in brighter (lighter) colors.
RB3-SLD.
The N-terminal module (module 1 or M1, colored cyan) comprises
residues 4 to 61; it interacts with α1, the “first” α subunit in
T2R. The following three modules, M2 (residues 62–83, colored
magenta), M3 (residues 84–112, colored light green) and M4
(residues 113–134, colored gray) respectively, interact with β1,
α2, and β2.
Tubulin
monomer (TR1-D2 structure). The α and β subunits are
shown along with D2 which is the crystallization chaperone. D2
targets the β tubulin longitudinal interface, hence its binding
site is distinct from that of R1 and the two proteins do no
interfere for tubulin binding. |