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<jats:p>Haspin is a mitotic protein kinase that is responsible for the phosphorylation of Thr3 of histone H3, thereby creating a recognition motif for docking of the chromosomal passenger complex that is crucial for the progression of cell division. Here, two high-resolution models of haspin with previously reported inhibitors consisting of an ATP analogue and a histone H3(1–7) peptide analogue are presented. The structures of the complexes confirm the bisubstrate character of the inhibitors by revealing the signature binding modes of the moieties targeting the ATP-binding site and the protein substrate-binding site of the kinase. This is the first structural model of a bisubstrate inhibitor targeting haspin. The presented structural data represent a model for the future development of more specific haspin inhibitors.</jats:p>

Original publication

DOI

10.1107/s2053230x16004611

Type

Journal article

Journal

Acta Crystallographica Section F Structural Biology Communications

Publisher

International Union of Crystallography (IUCr)

Publication Date

01/05/2016

Volume

72

Pages

339 - 345