2isd: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2isd.jpg|left|200px]]<br /><applet load="2isd" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2isd, resolution 2.5&Aring;" />
caption="2isd, resolution 2.5&Aring;" />
'''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, 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.
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 superseeds 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ISD OCA].  
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.O.]]
[[Category: Essen, L O.]]
[[Category: Perisic, O.]]
[[Category: Perisic, O.]]
[[Category: Williams, R.L.]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:26:02 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:55:26 2008''