4C2V

Aurora B kinase in complex with the specific inhibitor Barasertib

Summary for 4C2V

• Entry DOI: 10.2210/pdb4c2v/pdb
• Related: 4C2W
• Descriptor: AURORA KINASE B-A, INNER CENTROMERE PROTEIN A, 2-[5-[[7-[3-[ethyl(2-hydroxyethyl)amino]propoxy]quinazolin-4-yl]amino]-1H-pyrazol-3-yl]-N-(3-fluorophenyl)ethanamide, ... (4 entities in total)
• Functional Keywords: transferase-cell cycle complex, azd1152, transferase/cell cycle
• Biological source: XENOPUS LAEVIS (AFRICAN CLAWED FROG); More
• Cellular location: Nucleus: Q6DE08; Chromosome, centromere: O13024
• Total number of polymer chains: 4
• Total formula weight: 78464.47

Authors

Sessa, F.,Villa, F. (deposition date: 2013-08-20, release date: 2014-02-26, Last modification date: 2024-10-23)

Primary citation

Sessa, F.,Villa, F.
Structure of Aurora B-Incenp in Complex with Barasertib Reveals a Potential Transinhibitory Mechanism
Acta Crystallogr.,Sect.F, 70:294-, 2014

PubMed Abstract: The Aurora family is a well conserved and well characterized group of serine-threonine kinases involved in the normal progression of mitosis. The deregulation of Aurora kinases impairs spindle assembly, checkpoint function and cell division. To date, many small molecules that compete with ATP for binding to Aurora kinases have been developed and characterized. Here, the first structure of the Xenopus laevis Aurora B-INCENP complex bound to the clinically relevant small molecule barasertib was determined. The binding properties of this inhibitor to the Aurora B active site are analyzed and reported. An unexpected crystal-packing contact in the Aurora B-INCENP structure coordinated by an ATP analogue is also reported, in which the INCENP C-terminus occupies the substrate-binding region, resembling the protein kinase A inhibitory mechanism.

PubMed: 24598913
DOI: 10.1107/S2053230X14002118

Experimental method

X-RAY DIFFRACTION (1.49 Å)