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2isd

From Proteopedia

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{{STRUCTURE_2isd| PDB=2isd | SCENE= }}
{{STRUCTURE_2isd| PDB=2isd | SCENE= }}
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'''PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT'''
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===PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_8602259}}
==About this Structure==
==About this Structure==
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[[Category: Phosphoric diester hydrolase]]
[[Category: Phosphoric diester hydrolase]]
[[Category: Transducer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:46:14 2008''

Revision as of 12:46, 27 July 2008

Image:2isd.png

Template:STRUCTURE 2isd

PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT

Template:ABSTRACT PUBMED 8602259

About this Structure

2ISD is a Single protein structure of sequence from Rattus norvegicus. This structure supersedes the now removed PDB entry 1isd. Full crystallographic information is available from OCA.

Reference

Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta., Essen LO, Perisic O, Cheung R, Katan M, Williams RL, Nature. 1996 Apr 18;380(6575):595-602. PMID:8602259

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