2isd
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(New page: 200px<br /><applet load="2isd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2isd, resolution 2.5Å" /> '''PHOSPHOINOSITIDE-SPEC...)
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Revision as of 10:18, 21 November 2007
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PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT
Overview
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 Structure
2ISD is a Single protein structure of sequence from Rattus norvegicus with ACT as ligand. This structure superseeds the now removed PDB entry 1ISD. Active as Phosphoinositide phospholipase C, with EC number 3.1.4.11 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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