doi: 10.1038/380595a0.
Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
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- PMID: 8602259
- DOI: 10.1038/380595a0
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Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
Nature.
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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.
Comment in
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Phospholipid signalling. Taking stock of PI-PLC.Nature. 1996 Apr 18;380(6575):581-3. doi: 10.1038/380581a0. Nature. 1996. PMID: 8602254 No abstract available.
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