1mai

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[[Image:1mai.gif|left|200px]]
 
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==STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM PHOSPHOLIPASE C DELTA IN COMPLEX WITH INOSITOL TRISPHOSPHATE==
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The line below this paragraph, containing "STRUCTURE_1mai", creates the "Structure Box" on the page.
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<StructureSection load='1mai' size='340' side='right'caption='[[1mai]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1mai]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MAI FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene></td></tr>
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{{STRUCTURE_1mai| PDB=1mai | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mai OCA], [https://pdbe.org/1mai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mai RCSB], [https://www.ebi.ac.uk/pdbsum/1mai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mai ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ma/1mai_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1mai ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM PHOSPHOLIPASE C DELTA IN COMPLEX WITH INOSITOL TRISPHOSPHATE'''
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==See Also==
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*[[Phospholipase C|Phospholipase C]]
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__TOC__
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==Overview==
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</StructureSection>
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The X-ray crystal structure of the high affinity complex between the pleckstrin homology (PH) domain from rat phospholipase C-delta 1 (PLC-delta 1) and inositol-(1,4,5)-trisphosphate (Ins(1,4,5)P3) has been refined to 1.9 A resolution. The domain fold is similar to others of known structure. Ins(1,4,5)P3 binds on the positively charged face of the electrostatically polarized domain, interacting predominantly with the beta 1/beta 2 and beta 3/beta 4 loops. The 4- and 5-phosphate groups of Ins(1,4,5)P3 interact much more extensively than the 1-phosphate. Two amino acids in the PLC-delta 1 PH domain that contact Ins(1,4,5)P3 have counterparts in the Bruton's tyrosine kinase (Btk) PH domain, where mutational changes cause inherited agammaglobulinemia, suggesting a mechanism for loss of function in Btk mutants. Using electrostatics and varying levels of head-group specificity, PH domains may localize and orient signaling proteins, providing a general membrane targeting and regulatory function.
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[[Category: Large Structures]]
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==About this Structure==
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1MAI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAI OCA].
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==Reference==
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Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain., Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB, Cell. 1995 Dec 15;83(6):1037-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8521504 8521504]
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[[Category: Phosphoinositide phospholipase C]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Ferguson KM]]
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[[Category: Ferguson, K M.]]
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[[Category: Lemmon MA]]
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[[Category: Lemmon, M A.]]
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[[Category: Schlessinger J]]
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[[Category: Schlessinger, J.]]
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[[Category: Sigler PB]]
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[[Category: Sigler, P B.]]
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[[Category: Hydrolase]]
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[[Category: Inositol trisphosphate]]
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[[Category: Phospholipase]]
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[[Category: Pleckstrin]]
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[[Category: Signal transduction protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:49:35 2008''
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Current revision

STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM PHOSPHOLIPASE C DELTA IN COMPLEX WITH INOSITOL TRISPHOSPHATE

PDB ID 1mai

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