3kl8
From Proteopedia
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==CaMKIINtide Inhibitor Complex== | ==CaMKIINtide Inhibitor Complex== | ||
| - | <StructureSection load='3kl8' size='340' side='right' caption='[[3kl8]], [[Resolution|resolution]] 3.37Å' scene=''> | + | <StructureSection load='3kl8' size='340' side='right'caption='[[3kl8]], [[Resolution|resolution]] 3.37Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3kl8]] is a 10 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3kl8]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KL8 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.372Å</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=3kl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kl8 OCA], [https://pdbe.org/3kl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kl8 RCSB], [https://www.ebi.ac.uk/pdbsum/3kl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kl8 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kl/3kl8_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kl/3kl8_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=3kl8 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The dodecameric holoenzyme of calcium-calmodulin-dependent protein kinase II (CaMKII) responds to high-frequency Ca(2+) pulses to become Ca(2+) independent. A simple coincidence-detector model for Ca(2+)-frequency dependency assumes noncooperative activation of kinase domains. We show that activation of CaMKII by Ca(2+)-calmodulin is cooperative, with a Hill coefficient of approximately 3.0, implying sequential kinase-domain activation beyond dimeric units. We present data for a model in which cooperative activation includes the intersubunit 'capture' of regulatory segments. Such a capture interaction is seen in a crystal structure that shows extensive contacts between the regulatory segment of one kinase and the catalytic domain of another. These interactions are mimicked by a natural inhibitor of CaMKII. Our results show that a simple coincidence-detection model cannot be operative and point to the importance of kinetic dissection of the frequency-response mechanism in future experiments. | ||
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| - | Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation.,Chao LH, Pellicena P, Deindl S, Barclay LA, Schulman H, Kuriyan J Nat Struct Mol Biol. 2010 Mar;17(3):264-72. Epub 2010 Feb 7. PMID:20139983<ref>PMID:20139983</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Calcium/calmodulin dependent protein kinase 3D structures|Calcium/calmodulin dependent protein kinase 3D structures]] | |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: Barclay | + | [[Category: Barclay LA]] |
| - | [[Category: Chao | + | [[Category: Chao LH]] |
| - | [[Category: Deindl | + | [[Category: Deindl S]] |
| - | [[Category: Kuriyan | + | [[Category: Kuriyan J]] |
| - | [[Category: Pellicena | + | [[Category: Pellicena P]] |
| - | [[Category: Schulman | + | [[Category: Schulman H]] |
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Current revision
CaMKIINtide Inhibitor Complex
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