First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP5 kinase

Andrew M. Riley; Huanchen Wang; Jeremy D. Weaver; Stephen B. Shears; Barry V. L. Potter

doi:10.1039/c2cc36044f

First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP₅ kinase

Andrew M. Riley
, Huanchen Wang
, Jeremy D. Weaver
, Stephen B. Shears
, Barry V. L. Potter

Department of Life Sciences

Research output: Contribution to journal › Article › peer-review

34 Citations (SciVal)

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.

Original language	English
Pages (from-to)	11292-11294
Number of pages	3
Journal	Chemical Communications
Volume	48
Issue number	92
Early online date	17 Sept 2012
DOIs	https://doi.org/10.1039/c2cc36044f
Publication status	Published - 24 Oct 2012

Access to Document

10.1039/c2cc36044f

Cite this

@article{1640dcfd4a0e4f75bcde9802402976bd,

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.",

author = "Riley, \{Andrew M.\} and Huanchen Wang and Weaver, \{Jeremy D.\} and Shears, \{Stephen B.\} and Potter, \{Barry V. L.\}",

year = "2012",

month = oct,

day = "24",

doi = "10.1039/c2cc36044f",

language = "English",

volume = "48",

pages = "11292--11294",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "92",

}

TY - JOUR

T1 - First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP5 kinase

AU - Riley, Andrew M.

AU - Wang, Huanchen

AU - Weaver, Jeremy D.

AU - Shears, Stephen B.

AU - Potter, Barry V. L.

PY - 2012/10/24

Y1 - 2012/10/24

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/84867934187

UR - http://dx.doi.org/10.1039/c2cc36044f

U2 - 10.1039/c2cc36044f

DO - 10.1039/c2cc36044f

M3 - Article

SN - 1359-7345

VL - 48

SP - 11292

EP - 11294

JO - Chemical Communications

JF - Chemical Communications

IS - 92

ER -

First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP₅ kinase

Abstract

Access to Document

Other files and links

Fingerprint

Cite this