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. 1996 Apr 18;380(6575):595-602.
doi: 10.1038/380595a0.

Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta

L O Essen  1 , O Perisic, R Cheung, M Katan, R L Williams
Affiliations

Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta

L O Essen et al. Nature. .

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.

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