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Figure 3.
Figure 3. Structure of Aurora-A Bound to TPX2(A) View of
the complex between the catalytic domain of human Aurora
(AuroraΔN, yellow) and the N-terminal domain of TPX2 shown in
typical kinase orientation. An upstream stretch of TPX2 (red)
binds at the N-terminal lobe of Aurora-A, and a downstream
stretch (pink) binds between the two lobes. A dotted line in
pink marks the approximate path of the linker connecting the two
TPX2 stretches (disordered and not modeled).(B) View of the
complex after a 180° rotation about the vertical axis in
respect to view in (A) shows more clearly the two stretches of
TPX2 binding to Aurora-A.(C) The upstream stretch of TPX2 (red,
residues 7–21^TPX) binds at a hydrophobic surface groove
present in the N-terminal lobe of the kinase (gray cartoon,
yellow side chains). Details of the extensive interactions are
shown in the same orientation as in (B). Aurora-A residues are
labeled in black, and TPX2 residue labels are color coded as the
structure.(D) The downstream helical stretch of TPX2 (pink,
residues 30–43^TPX) binds Aurora-A near helix αC and the
activation segment, close to but not directly in contact with
phospho-Thr288^AUR (green). Details of interactions are shown in
the same orientation as in (B) and (C).
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