 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](hv5252fig2mag.jpg)
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Figure 2
The INCENP C-terminal extension occupies the Aurora B substrate-recognition surface. (a) The arrangement of Aurora B–INCENP molecules in the asymmetric unit is shown in cartoon and ribbon format in grey (Aurora B) and orange (INCENP). The C-terminal portion of INCENP packs against the Aurora B large C-lobe. (b) Details of the INCENP IN-box (orange) molecular interactions with the Aurora B kinase domain (grey). Calculated electron-density maps for the AMP-PNP and for the INCENP segment are drawn in green and brown, respectively. O, N and S atoms are shown in red, blue and yellow, respectively. (c) Multiple sequence alignment of the INCENP C-terminal region from different species. The alignment is colour-coded based on conservation. A solid red bar indicates the INCENP stretch occupying the Aurora B substrate-recognition surface. Numbering is according to the X. laevis sequence. (d, e) Surface representations of Aurora B with INCENP (d) and of protein kinase A with PKI (PDB entry 1atp ; Zheng et al., 1993  ) (e). Surfaces are coloured according to the electrostatic potential distribution of the kinases, ramped from blue (positive) to red (negative). (f) Schematic representation of an Aurora B potential transinhibitory model proceeding through an intermolecular mechanism, which may be enhanced by a high local protein concentration. This transinhibition mechanism may be relieved by a pTSS–pThr248 repulsion and lead to full activity of Aurora B. A Ser/Thr phosphatase can then revert the full Aurora B activity to a transinhibited state. |
![[Figure 2]](hv5252fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
