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2bfx
From Proteopedia
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| - | [[Image:2bfx.gif|left|200px]] | + | [[Image:2bfx.gif|left|200px]] |
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| - | '''MECHANISM OF AURORA-B ACTIVATION BY INCENP AND INHIBITION BY HESPERIDIN.''' | + | {{Structure |
| + | |PDB= 2bfx |SIZE=350|CAPTION= <scene name='initialview01'>2bfx</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''MECHANISM OF AURORA-B ACTIVATION BY INCENP AND INHIBITION BY HESPERIDIN.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BFX is a [ | + | 2BFX is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFX OCA]. |
==Reference== | ==Reference== | ||
| - | Mechanism of Aurora B activation by INCENP and inhibition by hesperadin., Sessa F, Mapelli M, Ciferri C, Tarricone C, Areces LB, Schneider TR, Stukenberg PT, Musacchio A, Mol Cell. 2005 Apr 29;18(3):379-91. PMID:[http:// | + | Mechanism of Aurora B activation by INCENP and inhibition by hesperadin., Sessa F, Mapelli M, Ciferri C, Tarricone C, Areces LB, Schneider TR, Stukenberg PT, Musacchio A, Mol Cell. 2005 Apr 29;18(3):379-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15866179 15866179] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
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[[Category: transferase complex]] | [[Category: transferase complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:01:24 2008'' |
Revision as of 14:01, 20 March 2008
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| , resolution 1.80Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
MECHANISM OF AURORA-B ACTIVATION BY INCENP AND INHIBITION BY HESPERIDIN.
Overview
Aurora family serine/threonine kinases control mitotic progression, and their deregulation is implicated in tumorigenesis. Aurora A and Aurora B, the best-characterized members of mammalian Aurora kinases, are approximately 60% identical but bind to unrelated activating subunits. The structure of the complex of Aurora A with the TPX2 activator has been reported previously. Here, we report the crystal structure of Aurora B in complex with the IN-box segment of the inner centromere protein (INCENP) activator and with the small molecule inhibitor Hesperadin. The Aurora B:INCENP complex is remarkably different from the Aurora A:TPX2 complex. INCENP forms a crown around the small lobe of Aurora B and induces the active conformation of the T loop allosterically. The structure represents an intermediate state of activation of Aurora B in which the Aurora B C-terminal segment stabilizes an open conformation of the catalytic cleft, and a critical ion pair in the kinase active site is impaired. Phosphorylation of two serines in the carboxyl terminus of INCENP generates the fully active kinase.
About this Structure
2BFX is a Protein complex structure of sequences from Xenopus laevis. Full crystallographic information is available from OCA.
Reference
Mechanism of Aurora B activation by INCENP and inhibition by hesperadin., Sessa F, Mapelli M, Ciferri C, Tarricone C, Areces LB, Schneider TR, Stukenberg PT, Musacchio A, Mol Cell. 2005 Apr 29;18(3):379-91. PMID:15866179
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