PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RATPHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT

Structural highlights

2isd is a 2 chain structure with sequence from Rattus norvegicus. This structure supersedes the now removed PDB entry 1isd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:CDNA FRAGMENT (Rattus norvegicus)
Activity:Phosphoinositide phospholipase C, with EC number 3.1.4.11
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Essen LO, Perisic O, Cheung R, Katan M, Williams RL. Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta. Nature. 1996 Apr 18;380(6575):595-602. PMID:8602259 doi:http://dx.doi.org/10.1038/380595a0

2isd, resolution 2.50Å

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