First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP(5) kinase

We synthesised analogues of diphosphoinositol polyphosphates (PP-InsPs) in which the diphosphate is replaced by an a-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...

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Bibliographic Details
Published inChemical communications (Cambridge, England) Vol. 48; no. 92; pp. 11292 - 11294
Main Authors Riley, Andrew M., Wang, Huanchen, Weaver, Jeremy D., Shears, Stephen B., Potter, Barry V. L.
Format Journal Article
LanguageEnglish
Published CAMBRIDGE Royal Soc Chemistry 30.07.2013
Subjects
Chemistry
Chemistry, Multidisciplinary
Physical Sciences
Science & Technology
DICTYOSTELIUM
CELLS
PENTAKISPHOSPHATE
MEDIATORS
BINDING
INOSITOL
PYROPHOSPHATES
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Summary:We synthesised analogues of diphosphoinositol polyphosphates (PP-InsPs) in which the diphosphate is replaced by an a-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.
Bibliography:NIH RePORTER
ISSN:1359-7345
DOI:10.1039/c2cc36044f