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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"
caption="2isd, resolution 2.5&Aring;" />
'''PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT'''<br />


==Overview==
==PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT==
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.
<StructureSection load='2isd' size='340' side='right'caption='[[2isd]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>


==About this Structure==
==See Also==
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].
*[[Phospholipase C|Phospholipase C]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8602259 8602259]
[[Category: Large Structures]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:26:02 2007''

Latest revision as of 09:04, 21 February 2024

PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT

2isd, resolution 2.50Å

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