Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
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DOI：
10.1038/380595a0
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发表时间：
1996-04-18
期刊：
影响因子：
64.8
通讯作者：
Williams, RL
中科院分区：
文献类型：
--
作者：
Essen, LO;Perisic, O;Williams, RL
哺乳动物磷酸肌醇特异性磷脂酶 C 酶 (PI-PLC) 充当信号转导器，产生两个第二信使：肌醇 1,4,5-三磷酸和二酰基甘油。磷脂酶 C delta 1 的 2.4 埃结构揭示了一种包含许多信号蛋白共享模块的多结构域蛋白。该结构表明了第二信使前体的膜附着和 Ca2+ 依赖性水解的机制。 PI-PLC 的调节和可逆膜关联可以作为理解参与磷脂信号传导的其他多域酶的模型。
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-Angstrom 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.