Phosphoinositide-specific phospholipase C: Structural basis for catalysis and regulatory interactions

被引：34

作者：

Katan, M ^{[1
]}

Williams, RL ^{[1
]}

机构：

[1] MRC,MOL BIOL LAB,CAMBRIDGE CB2 2QH,ENGLAND

来源：

SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY | 1997年 / 8卷 / 03期

基金：

英国医学研究理事会;

关键词：

catalysis; G-proteins; phosphoinositide-specific phospholipase C (PI-PLC); three-dimensional structure; tyrosine kinase receptors;

D O I：

10.1006/scdb.1997.0150

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Phosphoinositide-specific phospholipase C (PI-PLC) isozymes have an important role in cellular responses to a variety of extracellular signals. Recently the three-dimensional structures of their isolated domains and of the multidomain core, common to all PI-PLCs, have been solved. This provided an insight into the domain organization of PI-PLCs and, together with the structure-function analysis, contributed towards an understanding of the molecular mechanisms of catalysis and regulation.

引用

页码：287 / 296

页数：10

共 66 条

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BANNO Y, 1994, J BIOL CHEM, V269, P15846

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