2isd
From Proteopedia
(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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| - | [[Image:2isd.jpg|left|200px]]<br /><applet load="2isd" size=" | + | [[Image:2isd.jpg|left|200px]]<br /><applet load="2isd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2isd, resolution 2.5Å" /> | caption="2isd, resolution 2.5Å" /> | ||
'''PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT'''<br /> | '''PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Mammalian phosphoinositide-specific phospholipase C enzymes (PI-PLC) act | + | 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== | ==About this Structure== | ||
| - | 2ISD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 2ISD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1ISD. Active as [http://en.wikipedia.org/wiki/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ISD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Essen, L | + | [[Category: Essen, L O.]] |
[[Category: Perisic, O.]] | [[Category: Perisic, O.]] | ||
| - | [[Category: Williams, R | + | [[Category: Williams, R L.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: calcium-binding]] | [[Category: calcium-binding]] | ||
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[[Category: transducer]] | [[Category: transducer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:55:26 2008'' |
Revision as of 15:55, 21 February 2008
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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 as ligand. This structure supersedes 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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