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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2001-5-11
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pubmed:abstractText |
Inositol polyphosphate 5-phosphatases are central to intracellular processes ranging from membrane trafficking to Ca(2+) signaling, and defects in this activity result in the human disease Lowe syndrome. The 1.8 resolution structure of the inositol polyphosphate 5-phosphatase domain of SPsynaptojanin bound to Ca(2+) and inositol (1,4)-bisphosphate reveals a fold and an active site His and Asp pair resembling those of several Mg(2+)-dependent nucleases. Additional loops mediate specific inositol polyphosphate contacts. The 4-phosphate of inositol (1,4)-bisphosphate is misoriented by 4.6 compared to the reactive geometry observed in the apurinic/apyrimidinic endonuclease 1, explaining the dephosphorylation site selectivity of the 5-phosphatases. Based on the structure, a series of mutants are described that exhibit altered substrate specificity providing general determinants for substrate recognition.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/inositol 1,4-bis(phosphate),
http://linkedlifedata.com/resource/pubmed/chemical/inositol-1,4,5-trisphosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/synaptojanin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
379-89
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11348594-Amino Acid Sequence,
pubmed-meshheading:11348594-Binding Sites,
pubmed-meshheading:11348594-Calcium,
pubmed-meshheading:11348594-Catalytic Domain,
pubmed-meshheading:11348594-Cloning, Molecular,
pubmed-meshheading:11348594-Crystallography, X-Ray,
pubmed-meshheading:11348594-Enzyme Inhibitors,
pubmed-meshheading:11348594-Humans,
pubmed-meshheading:11348594-Inositol Phosphates,
pubmed-meshheading:11348594-Models, Molecular,
pubmed-meshheading:11348594-Molecular Sequence Data,
pubmed-meshheading:11348594-Mutation,
pubmed-meshheading:11348594-Nerve Tissue Proteins,
pubmed-meshheading:11348594-Phosphoric Monoester Hydrolases,
pubmed-meshheading:11348594-Phosphorylation,
pubmed-meshheading:11348594-Protein Conformation,
pubmed-meshheading:11348594-Protein Folding,
pubmed-meshheading:11348594-Protein Structure, Quaternary,
pubmed-meshheading:11348594-Protein Structure, Secondary,
pubmed-meshheading:11348594-Protein Structure, Tertiary,
pubmed-meshheading:11348594-Recombinant Proteins,
pubmed-meshheading:11348594-Schizosaccharomyces,
pubmed-meshheading:11348594-Sequence Alignment,
pubmed-meshheading:11348594-Substrate Specificity
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pubmed:year |
2001
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pubmed:articleTitle |
Specificity determinants in phosphoinositide dephosphorylation: crystal structure of an archetypal inositol polyphosphate 5-phosphatase.
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pubmed:affiliation |
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, , Bethesda, MD 20892, USA.
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pubmed:publicationType |
Journal Article
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