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[[Image:2isd.jpg|left|200px]]


{{Structure
==PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT==
|PDB= 2isd |SIZE=350|CAPTION= <scene name='initialview01'>2isd</scene>, resolution 2.5&Aring;
<StructureSection load='2isd' size='340' side='right'caption='[[2isd]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene>
<table><tr><td colspan='2'>[[2isd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1isd 1isd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ISD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ISD FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
|GENE= CDNA FRAGMENT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2isd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2isd OCA], [https://pdbe.org/2isd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2isd RCSB], [https://www.ebi.ac.uk/pdbsum/2isd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2isd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PLCD1_RAT PLCD1_RAT] The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Essential for trophoblast and placental development.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/is/2isd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2isd ConSurf].
<div style="clear:both"></div>


'''PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT'''
==See Also==
 
*[[Phospholipase C|Phospholipase C]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
2ISD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry 1ISD. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ISD 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:[http://www.ncbi.nlm.nih.gov/pubmed/8602259 8602259]
[[Category: Phosphoinositide phospholipase C]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Essen L-O]]
[[Category: Essen, L O.]]
[[Category: Perisic O]]
[[Category: Perisic, O.]]
[[Category: Williams RL]]
[[Category: Williams, R L.]]
[[Category: ACT]]
[[Category: calcium-binding]]
[[Category: hydrolase]]
[[Category: lipid degradation]]
[[Category: phosphoinositide-specific]]
[[Category: phospholipase c]]
[[Category: phosphoric diester hydrolase]]
[[Category: transducer]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:32:45 2008''

Latest revision as of 12:04, 21 February 2024

PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RATPHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT

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.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PLCD1_RAT The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Essential for trophoblast and placental development.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2isd, resolution 2.50Å

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