Document Detail

First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP5 kinase.
MedLine Citation:
PMID:  23032903     Owner:  NLM     Status:  MEDLINE    
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.
Andrew M Riley; Huanchen Wang; Jeremy D Weaver; Stephen B Shears; Barry V L Potter
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Chemical communications (Cambridge, England)     Volume:  48     ISSN:  1364-548X     ISO Abbreviation:  Chem. Commun. (Camb.)     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-10-25     Completed Date:  2013-03-28     Revised Date:  2014-02-17    
Medline Journal Info:
Nlm Unique ID:  9610838     Medline TA:  Chem Commun (Camb)     Country:  England    
Other Details:
Languages:  eng     Pagination:  11292-4     Citation Subset:  IM    
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MeSH Terms
Binding Sites
Catalytic Domain
Crystallography, X-Ray
Inositol Phosphates / chemistry
Phosphotransferases (Phosphate Group Acceptor) / chemistry,  metabolism*
Polyphosphates / chemistry,  metabolism*
Substrate Specificity
Grant Support
082837//Wellcome Trust; Z01 ES080046-19/ES/NIEHS NIH HHS
Reg. No./Substance:
0/Inositol Phosphates; 0/Polyphosphates; EC 2.7.4.-/Phosphotransferases (Phosphate Group Acceptor); EC 2.7.4.-/diphosphoinositol pentakisphosphate kinase

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