 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](hv5252fig1mag.jpg)
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Figure 1
Binding of barasertib to the ATP-binding pocket of Aurora B. (a) Chemical structure of barasertib prodrug (red) and the active form (green). (b) The three-dimensional structure of Aurora B in cartoon representation, illustrating the N-terminal small lobe (grey), the C-terminal helical large lobe (white), the short C-terminal extension (green), the αC helix (blue) and the activation loop (red). INCENP (orange) crowns the small lobe of Aurora B, stabilizing an active conformation of the kinase. The active form of barasertib (sticks) and its unbiased Fo − Fc OMIT electron-density map (grey mesh) occupy the ATP-binding pocket at the interface between the small and large lobes. (c) Stick representation of the interaction between the active form of barasertib (green) and selected residues of Aurora B. (d) Structure superimposition of the Aurora B–INCENP–barasertib active form complex (grey) with the Aurora A–TPX-2 complex (cyan; PDB entry 1ol5 ; Bayliss et al., 2003  ). O, N and S atoms are shown in red, blue and yellow, respectively. Hydrogen bonds are shown as dashed lines and bond lengths are indicated in Å. |
![[Figure 1]](hv5252fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
