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PMID: 8602259 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta.

Nature ·Vol. 380 ·No. 6575 ·1996-04-18 ·Pages 595-602

Essen LO, Perisic O, Cheung R, Katan M, Williams RL

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.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Catalysis Cell Membrane/metabolism Crystallography, X-Ray Humans Hydrolysis Inositol 1,4,5-Trisphosphate/metabolism Isoenzymes/chemistry,metabolism Models, Molecular Molecular Conformation Molecular Sequence Data Phosphoinositide Phospholipase C Phospholipase C delta Phosphoric Diester Hydrolases/chemistry,metabolism Protein Binding Protein Conformation Rats Recombinant Proteins/chemistry,metabolism Second Messenger Systems Sequence Homology, Amino Acid
Chemicals
Isoenzymes Recombinant Proteins Inositol 1,4,5-Trisphosphate Phosphoric Diester Hydrolases Phosphoinositide Phospholipase C Phospholipase C delta
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Essen L O
Center for Protein Engineering, MRC Centre, Cambridge, UK.
Perisic O
Cheung R
Katan M
Williams R L
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1996-04-18
Pages
595-602
Language
English
Region
England
NLM ID
0410462
Subset
IM
Grants
Medical Research Council · MC_U105184308 · United Kingdom
Corrections
CommentIn
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