Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta

被引：506

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

页码：595 / 602

页数：8

共 50 条

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