Journal
CHEMICAL COMMUNICATIONS
Volume 48, Issue 92, Pages 11292-11294Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c2cc36044f
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Funding
- Wellcome Trust [082837]
- NIEHS/NIH
- U. S. Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]
- NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES [ZIAES080046] Funding Source: NIH RePORTER
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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.
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