Crystal Structure of Human Aurora B in Complex with INCENP and VX-680 | Zendy

Jonathan M. Elkins | Zendy; Stefano Santaguida | Zendy; Andrea Musacchio | Zendy; Stefan Knapp | Zendy

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Crystal Structure of Human Aurora B in Complex with INCENP and VX-680

Author(s) -

Jonathan M. Elkins,

Stefano Santaguida,

Andrea Musacchio,

Stefan Knapp

Publication year - 2012

Publication title -

journal of medicinal chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.01

H-Index - 261

eISSN - 1520-4804

pISSN - 0022-2623

DOI - 10.1021/jm3008954

Subject(s) - chemistry , xenopus , aurora b kinase , protein kinase domain , kinase , microbiology and biotechnology , aurora kinase , biochemistry , biology , cell cycle , apoptosis , kinetochore , mutant , chromosome , gene

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.

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