2isd | pdb_00002isd

PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT

spinqualitylabelsall models 2isd, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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: ACT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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