3kk9: Difference between revisions
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==CaMKII Substrate Complex B== | |||
=== | <StructureSection load='3kk9' size='340' side='right' caption='[[3kk9]], [[Resolution|resolution]] 3.21Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3kk9]] is a 1 chain structure with 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=3KK9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KK9 FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kk8|3kk8]], [[3kl8|3kl8]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">unc-43, K11E8.1, K11E8.1d ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kk9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kk9 RCSB], [http://www.ebi.ac.uk/pdbsum/3kk9 PDBsum]</span></td></tr> | |||
</table> | |||
== 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/kk/3kk9_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
[[Category: Barclay, L A | [[Category: Barclay, L A]] | ||
[[Category: Chao, L H | [[Category: Chao, L H]] | ||
[[Category: Deindl, S | [[Category: Deindl, S]] | ||
[[Category: Kuriyan, J | [[Category: Kuriyan, J]] | ||
[[Category: Pellicena, P | [[Category: Pellicena, P]] | ||
[[Category: Schulman, H | [[Category: Schulman, H]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Camkii]] | [[Category: Camkii]] | ||
Revision as of 19:06, 18 December 2014
CaMKII Substrate Complex BCaMKII Substrate Complex B
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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