2f86

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{{Seed}}
 
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[[Image:2f86.png|left|200px]]
 
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==The Association Domain of C. elegans CaMKII==
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The line below this paragraph, containing "STRUCTURE_2f86", creates the "Structure Box" on the page.
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<StructureSection load='2f86' size='340' side='right'caption='[[2f86]], [[Resolution|resolution]] 2.64&Aring;' scene=''>
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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'>[[2f86]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F86 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]] 2.64&#8491;</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=2f86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f86 OCA], [https://pdbe.org/2f86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f86 RCSB], [https://www.ebi.ac.uk/pdbsum/2f86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f86 ProSAT]</span></td></tr>
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{{STRUCTURE_2f86| PDB=2f86 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KCC2D_CAEEL KCC2D_CAEEL] Acts in the signaling of a variety of pathways and processes. Phosphorylates 'Ser-319' of daf-16 in response to stress signals, such as heat, starvation and oxidation, which plays a role in prolonging lifespan. Required for viability under chronic osmotic stress in which it acts downstream of osr-1. Has roles in locomotion, oocyte maturation, brood size, egg laying, defecation, meiotic maturation and neuronal cell fate specification. Required for the regulation of synaptic density and neuromuscular junction morphology. Regulates the synaptic trafficking of glr-1. Bidirectional modulator of neurotransmitter release with negative modulatory effects mainly mediated via slo-1 activation. Involved in activation of ADF neurons and increased tph-1 transcription following exposure to pathogenic bacteria which leads to learned olfactory aversion to the bacteria. Implicated in the muscle regulation of spicule protraction. In conjunction with egl-2 has a role in the suppression of mating behavior under food deprivation to encourage foraging. Involved in restricting str-2 expression to only one of the two AWC neurons. May suppress the functional response to an internal pacemaker, perhaps by modulating the activity of the IP3 receptor.<ref>PMID:10571181</ref> <ref>PMID:12221132</ref> <ref>PMID:15166144</ref> <ref>PMID:16079277</ref> <ref>PMID:16267094</ref> <ref>PMID:17898212</ref> <ref>PMID:17941711</ref> <ref>PMID:17942636</ref> <ref>PMID:21145946</ref> <ref>PMID:21771813</ref> <ref>PMID:22629462</ref> <ref>PMID:23325232</ref> <ref>PMID:23663262</ref> <ref>PMID:23805378</ref>
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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/f8/2f86_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=2f86 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ca2+/calmodulin activated protein kinase II (CaMKII) is an oligomeric protein kinase with a unique holoenyzme architecture. The subunits of CaMKII are bound together into the holoenzyme by the association domain, a C-terminal region of approximately 140 residues in the CaMKII polypeptide. Single particle analyses of electron micrographs have suggested previously that the holoenyzme forms a dodecamer that contains two stacked 6-fold symmetric rings. In contrast, a recent crystal structure of the isolated association domain of mouse CaMKIIalpha has revealed a tetradecameric assembly with two stacked 7-fold symmetric rings. In this study, we have determined the crystal structure of the Caenorhabditis elegans CaMKII association domain and it too forms a tetradecamer. We also show by electron microscopy that in its fully assembled form the CaMKII holoenzyme is a dodecamer but without the kinase domains, either from expression of the isolated association domain in bacteria or following their removal by proteolysis, the association domains form a tetradecamer. We speculate that the holoenzyme is held in its 6-fold symmetric state by the interactions of the N-terminal approximately 1-335 residues and that the removal of this region allows the association domain to convert into a more stable 7-fold symmetric form.
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===The Association Domain of C. elegans CaMKII===
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Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II.,Rosenberg OS, Deindl S, Comolli LR, Hoelz A, Downing KH, Nairn AC, Kuriyan J FEBS J. 2006 Feb;273(4):682-94. PMID:16441656<ref>PMID:16441656</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_16441656}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2f86" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16441656 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16441656}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2F86 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F86 OCA].
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==Reference==
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Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II., Rosenberg OS, Deindl S, Comolli LR, Hoelz A, Downing KH, Nairn AC, Kuriyan J, FEBS J. 2006 Feb;273(4):682-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16441656 16441656]
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[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kuriyan, J.]]
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[[Category: Kuriyan J]]
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[[Category: Rosenberg, O S.]]
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[[Category: Rosenberg OS]]
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[[Category: Oligomerization domain]]
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[[Category: Unc-43]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:01:27 2008''
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Current revision

The Association Domain of C. elegans CaMKII

PDB ID 2f86

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