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5u6y

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Current revision (15:45, 6 March 2024) (edit) (undo)
 
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<SX load='5u6y' size='340' side='right' viewer='molstar' caption='[[5u6y]], [[Resolution|resolution]] 20.00&Aring;' scene=''>
<SX load='5u6y' size='340' side='right' viewer='molstar' caption='[[5u6y]], [[Resolution|resolution]] 20.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5u6y]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U6Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5U6Y FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5u6y]] is a 12 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=5U6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5U6Y FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Camk2a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 20&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium/calmodulin-dependent_protein_kinase Calcium/calmodulin-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.17 2.7.11.17] </span></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=5u6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u6y OCA], [https://pdbe.org/5u6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5u6y RCSB], [https://www.ebi.ac.uk/pdbsum/5u6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5u6y ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5u6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u6y OCA], [http://pdbe.org/5u6y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u6y RCSB], [http://www.ebi.ac.uk/pdbsum/5u6y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u6y ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/KCC2A_RAT KCC2A_RAT]] CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses it may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity.<ref>PMID:15312654</ref>
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[https://www.uniprot.org/uniprot/KCC2A_RAT KCC2A_RAT] CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses it may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity.<ref>PMID:15312654</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Ca2+/calmodulin-dependent protein kinase II (CaMKII) assembles into large 12-meric holoenzymes, which is thought to enable regulatory processes required for synaptic plasticity underlying learning, memory and cognition. Here we used single particle electron microscopy (EM) to determine a pseudoatomic model of the CaMKIIalpha holoenzyme in an extended and activation-competent conformation. The holoenzyme is organized by a rigid central hub complex, while positioning of the kinase domains is highly flexible, revealing dynamic holoenzymes ranging from 15-35 nm in diameter. While most kinase domains are ordered independently, approximately 20% appear to form dimers and &lt;3% are consistent with a compact conformation. An additional level of plasticity is revealed by a small fraction of bona-fide 14-mers (&lt;4%) that may enable subunit exchange. Biochemical and cellular FRET studies confirm that the extended state of CaMKIIalpha resolved by EM is the predominant form of the holoenzyme, even under molecular crowding conditions.
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The CaMKII holoenzyme structure in activation-competent conformations.,Myers JB, Zaegel V, Coultrap SJ, Miller AP, Bayer KU, Reichow SL Nat Commun. 2017 Jun 7;8:15742. doi: 10.1038/ncomms15742. PMID:28589927<ref>PMID:28589927</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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</div>
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<div class="pdbe-citations 5u6y" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
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[[Category: Buffalo rat]]
 
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[[Category: Calcium/calmodulin-dependent protein kinase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Myers, J]]
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[[Category: Rattus norvegicus]]
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[[Category: Reichow, S L]]
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[[Category: Myers J]]
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[[Category: Calcium]]
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[[Category: Reichow SL]]
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[[Category: Cell signaling]]
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[[Category: Cooperativity]]
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[[Category: Intrinsic disorder]]
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[[Category: Single particle reconstruction]]
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[[Category: Synaptic plasticity]]
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[[Category: Transferase]]
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Current revision

Pseudo-atomic model of the CaMKIIa holoenzyme.

5u6y, resolution 20.00Å

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