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We synthesised analogues of diphosphoinositol polyphosphates (PP-InsPs) in which the diphosphate is replaced by an α-phosphonoacetic acid (PA) ester. Structural analysis revealed that 5-PA-InsP(5) mimics 5-PP-InsP(5) binding to the kinase domain of PPIP5K2; both molecules were phosphorylated by the enzyme. PA-InsPs are promising candidates for further studies into the biology of PP-InsPs.

Original publication

DOI

10.1039/c2cc36044f

Type

Journal article

Journal

Chem Commun (Camb)

Publication Date

28/11/2012

Volume

48

Pages

11292 - 11294

Keywords

Binding Sites, Biocatalysis, Catalytic Domain, Crystallography, X-Ray, Humans, Inositol Phosphates, Phosphotransferases (Phosphate Group Acceptor), Polyphosphates, Substrate Specificity