Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta

被引：503
|
作者：
Essen, LO
Perisic, O
Cheung, R
Katan, M
Williams, RL
机构：
[1] UNIV CAMBRIDGE, CTR MRC, CTR PROT RES, CAMBRIDGE CB2 2QH, ENGLAND
[2] INST CANC RES, CHESTER BEATTY LABS, CRC, CTR CELL & MOL BIOL, LONDON SW3 6JB, ENGLAND
来源：
NATURE | 1996年 / 380卷 / 6575期
基金：
英国医学研究理事会;
关键词：
D O I：
10.1038/380595a0
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
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.
引用
收藏
页码：595 / 602
页数：8
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