1mai

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(New page: 200px<br /><applet load="1mai" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mai, resolution 1.90&Aring;" /> '''STRUCTURE OF THE PLE...)
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[[Image:1mai.gif|left|200px]]<br /><applet load="1mai" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mai, resolution 1.90&Aring;" />
 
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'''STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM PHOSPHOLIPASE C DELTA IN COMPLEX WITH INOSITOL TRISPHOSPHATE'''<br />
 
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==Overview==
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==STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM PHOSPHOLIPASE C DELTA IN COMPLEX WITH INOSITOL TRISPHOSPHATE==
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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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<StructureSection load='1mai' size='340' side='right'caption='[[1mai]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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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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</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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<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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==About this Structure==
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==See Also==
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1MAI 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 I3P as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1MAI OCA].
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*[[Phospholipase C|Phospholipase C]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8521504 8521504]
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[[Category: Large Structures]]
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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: I3P]]
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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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:16:42 2007''
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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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