Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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