2zkm: Difference between revisions

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


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==Crystal Structure of Phospholipase C Beta 2==
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<StructureSection load='2zkm' size='340' side='right'caption='[[2zkm]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2zkm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZKM FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.62&#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=CA:CALCIUM+ION'>CA</scene></td></tr>
{{STRUCTURE_2zkm|  PDB=2zkm  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zkm OCA], [https://pdbe.org/2zkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zkm RCSB], [https://www.ebi.ac.uk/pdbsum/2zkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zkm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PLCB2_HUMAN PLCB2_HUMAN] 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.
== 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/zk/2zkm_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=2zkm ConSurf].
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== Publication Abstract from PubMed ==
Phospholipase C (PLC) isozymes are directly activated by heterotrimeric G proteins and Ras-like GTPases to hydrolyze phosphatidylinositol 4,5-bisphosphate into the second messengers diacylglycerol and inositol 1,4,5-trisphosphate. Although PLCs play central roles in myriad signaling cascades, the molecular details of their activation remain poorly understood. As described here, the crystal structure of PLC-beta2 illustrates occlusion of the active site by a loop separating the two halves of the catalytic TIM barrel. Removal of this insertion constitutively activates PLC-beta2 without ablating its capacity to be further stimulated by classical G protein modulators. Similar regulation occurs in other PLC members, and a general mechanism of interfacial activation at membranes is presented that provides a unifying framework for PLC activation by diverse stimuli.


===Crystal Structure of Phospholipase C Beta 2===
General and versatile autoinhibition of PLC isozymes.,Hicks SN, Jezyk MR, Gershburg S, Seifert JP, Harden TK, Sondek J Mol Cell. 2008 Aug 8;31(3):383-94. PMID:18691970<ref>PMID:18691970</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2zkm" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_17115053}}, adds the Publication Abstract to the page
*[[Phospholipase C|Phospholipase C]]
(as it appears on PubMed at http://www.pubmed.gov), where 17115053 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_17115053}}
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</StructureSection>
==About this Structure==
2ZKM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZKM OCA].
 
==Reference==
Crystal structure of Rac1 bound to its effector phospholipase C-beta2., Jezyk MR, Snyder JT, Gershberg S, Worthylake DK, Harden TK, Sondek J, Nat Struct Mol Biol. 2006 Dec;13(12):1135-40. Epub 2006 Nov 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17115053 17115053]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Phosphoinositide phospholipase C]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Gershberg S]]
[[Category: Gershberg, S.]]
[[Category: Harden TK]]
[[Category: Harden, T K.]]
[[Category: Hicks SN]]
[[Category: Hicks, S N.]]
[[Category: Jezyk MR]]
[[Category: Jezyk, M R.]]
[[Category: Seifert JP]]
[[Category: Seifert, J P.]]
[[Category: Sondek J]]
[[Category: Sondek, J.]]
[[Category: Calcium]]
[[Category: Coiled coil]]
[[Category: Hydrolase]]
[[Category: Lipid degradation]]
[[Category: Metal-binding]]
[[Category: Phosphoinositide phospholipase]]
[[Category: Phospholipase c]]
[[Category: Plc-beta-2]]
[[Category: Transducer]]
 
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