2isd
PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Gene: | CDNA FRAGMENT (Rattus norvegicus) | ||||||
| Activity: | Phosphoinositide phospholipase C, with EC number 3.1.4.11 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout 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.
ReferenceReference
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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