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 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...

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Detalles Bibliográficos
Autores principales: Riley, Andrew M., Wang, Huanchen, Weaver, Jeremy D., Shears, Stephen B., Potter, Barry V. L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2012
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3923271/
https://www.ncbi.nlm.nih.gov/pubmed/23032903
http://dx.doi.org/10.1039/c2cc36044f
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author Riley, Andrew M.
Wang, Huanchen
Weaver, Jeremy D.
Shears, Stephen B.
Potter, Barry V. L.
author_facet Riley, Andrew M.
Wang, Huanchen
Weaver, Jeremy D.
Shears, Stephen B.
Potter, Barry V. L.
author_sort Riley, Andrew M.
collection PubMed
description 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.
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spelling pubmed-39232712014-02-13 First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP(5) kinase Riley, Andrew M. Wang, Huanchen Weaver, Jeremy D. Shears, Stephen B. Potter, Barry V. L. Chem Commun (Camb) Chemistry 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. Royal Society of Chemistry 2012-10-24 2012-10-03 /pmc/articles/PMC3923271/ /pubmed/23032903 http://dx.doi.org/10.1039/c2cc36044f Text en This journal is © The Royal Society of Chemistry 2012 http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Chemistry
Riley, Andrew M.
Wang, Huanchen
Weaver, Jeremy D.
Shears, Stephen B.
Potter, Barry V. L.
First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP(5) kinase
title First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP(5) kinase
title_full First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP(5) kinase
title_fullStr First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP(5) kinase
title_full_unstemmed First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP(5) kinase
title_short First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP(5) kinase
title_sort first synthetic analogues of diphosphoinositol polyphosphates: interaction with pp-insp(5) kinase
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3923271/
https://www.ncbi.nlm.nih.gov/pubmed/23032903
http://dx.doi.org/10.1039/c2cc36044f
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