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Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta.

Authors: Essen, L O  Perisic, O  Cheung, R  Katan, M  Williams, R L 
Citation: Essen LO, etal., Nature. 1996 Apr 18;380(6575):595-602.
Pubmed: (View Article at PubMed) PMID:8602259
DOI: Full-text: DOI:10.1038/380595a0

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.

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RGD Object Information
RGD ID: 12792989
Created: 2017-03-18
Species: All species
Last Modified: 2017-03-18
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.