Abstract
Mammalian phosphoinositide-specific phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The 2.4-A structure of phospholipase C delta 1 reveals a multidomain protein incorporating modules shared by many signalling proteins. The structure suggests a mechanism for membrane attachment and Ca2+-dependent hydrolysis of second-messenger precursors. The regulation and reversible membrane association of PI-PLC may serve as a model for understanding other multidomain enzymes involved in phospholipid signalling.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Catalysis
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Cell Membrane / metabolism
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Crystallography, X-Ray
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Humans
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Hydrolysis
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Inositol 1,4,5-Trisphosphate / metabolism
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Isoenzymes / chemistry*
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Isoenzymes / metabolism
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Models, Molecular
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Molecular Conformation
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Molecular Sequence Data
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Phosphoinositide Phospholipase C
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Phospholipase C delta
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Phosphoric Diester Hydrolases / chemistry*
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Phosphoric Diester Hydrolases / metabolism
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Protein Binding
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Protein Conformation
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Rats
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Second Messenger Systems
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Sequence Homology, Amino Acid
Substances
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Isoenzymes
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Recombinant Proteins
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Inositol 1,4,5-Trisphosphate
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Phosphoric Diester Hydrolases
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Phosphoinositide Phospholipase C
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Phospholipase C delta