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Figure 5.
Figure 5. TPX2-Aurora-A Intermolecular Interactions
Resemble cAPK Intramolecular Interactions(A and B) Transparent
surfaces representing the conserved catalytic cores of (A)
Aurora-A and (B) cAPK show similar surface grooves in the
N-terminal lobe (between helix αC and the β sheet, gray
cartoon) and a similar pocket between the two lobes (formed by
the activation segment and helix αC, gray cartoon). The
portions of TPX2 binding to Aurora-A are shown in red and pink
(A), and the N- and C-terminal extensions to the cAPK catalytic
core are shown in light blue (B).(C and D) Schematic diagram of
the intermolecular interactions between Aurora-A and TPX2 (pink
and red) and of the cAPK intramolecular interactions (light
blue) shows that their mode of recognition at the atomic level
is rather similar. The hydrophobic interactions of Tyr8^TPX,
Tyr10^TPX, Trp34^TPX, and Phe35^TPX are recapitulated by
Phe347^cAPK, Phe350^cAPK, Trp30^cAPK, and Phe26^cAPK.
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