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We present the structure of the human Aurora B kinase domain in complex with the C-terminal Aurora-binding region of human INCENP and the Aurora kinase inhibitor VX-680. The structure unexpectedly reveals a dimeric arrangement of the Aurora B:INCENP complex, which was confirmed to exist in solution by analytical ultracentrifugation. The dimerization involves a domain swap of the activation loop, resulting in a different conformation of the DFG motif as compared to that seen in other kinase complexes with VX-680. The binding of INCENP differs significantly from that seen in the Xenopus laevis Aurora B:INCENP complex currently used as a model for structure-based design for this important oncology target.

Original publication




Journal article


J Med Chem

Publication Date





7841 - 7848


Amino Acid Sequence, Aurora Kinase B, Aurora Kinases, Chromosomal Proteins, Non-Histone, Humans, Models, Molecular, Molecular Sequence Data, Piperazines, Protein-Serine-Threonine Kinases, Sequence Homology, Amino Acid