Structural highlights
Publication Abstract from PubMed
We synthesised analogues of diphosphoinositol polyphosphates (PP-InsPs) in which the diphosphate is replaced by an alpha-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.
First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP(5) kinase.,Riley AM, Wang H, Weaver JD, Shears SB, Potter BV Chem Commun (Camb). 2012 Oct 3. PMID:23032903[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Riley AM, Wang H, Weaver JD, Shears SB, Potter BV. First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP(5) kinase. Chem Commun (Camb). 2012 Oct 3. PMID:23032903 doi:http://dx.doi.org/10.1039/c2cc36044f