title: First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP5 kinase.
abstract: 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.
authors.affiliation: Wolfson Laboratory of Medicinal Chemistry, Department of Pharmacy and Pharmacology, University of Bath, BA2 7AY, UK.
authors.forename: Andrew M
authors.initials: AM
authors.lastname: Riley
authors.forename: Huanchen
authors.initials: H
authors.lastname: Wang
authors.forename: Jeremy D
authors.initials: JD
authors.lastname: Weaver
authors.forename: Stephen B
authors.initials: SB
authors.lastname: Shears
authors.forename: Barry V L
authors.initials: BV
authors.lastname: Potter
mesh_terms: D001665:Binding Sites; D055162:Biocatalysis; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006801:Humans; D007295:Inositol Phosphates / Q000737:chemistry; D017856:Phosphotransferases (Phosphate Group Acceptor) / Q000737:chemistry / Q000378:metabolism*; D011122:Polyphosphates / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D007295:Inositol Phosphates; D011122:Polyphosphates; D017856:Phosphotransferases (Phosphate Group Acceptor); C407349:diphosphoinositol pentakisphosphate kinase