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==Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B==
<StructureSection load='7ujr' size='340' side='right'caption='[[7ujr]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ujr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6xdl 6xdl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UJR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=7ujr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ujr OCA], [https://pdbe.org/7ujr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ujr RCSB], [https://www.ebi.ac.uk/pdbsum/7ujr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ujr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KCC2A_HUMAN KCC2A_HUMAN] 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 (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is a signaling protein required for long-term memory. When activated by Ca(2+)/CaM, it sustains activity even after the Ca(2+) dissipates. In addition to the well-known autophosphorylation-mediated mechanism, interaction with specific binding partners also persistently activates CaMKII. A long-standing model invokes two distinct S and T sites. If an interactor binds at the T-site, then it will preclude autoinhibition and allow substrates to be phosphorylated at the S site. Here, we specifically test this model with X-ray crystallography, molecular dynamics simulations, and biochemistry. Our data are inconsistent with this model. Co-crystal structures of four different activators or substrates show that they all bind to a single continuous site across the kinase domain. We propose a mechanistic model where persistent CaMKII activity is facilitated by high-affinity binding partners that kinetically compete with autoinhibition by the regulatory segment to allow substrate phosphorylation.

CaMKII binds both substrates and activators at the active site.,Ozden C, Sloutsky R, Mitsugi T, Santos N, Agnello E, Gaubitz C, Foster J, Lapinskas E, Esposito EA, Saneyoshi T, Kelch BA, Garman SC, Hayashi Y, Stratton MM Cell Rep. 2022 Jul 12;40(2):111064. doi: 10.1016/j.celrep.2022.111064. PMID:35830796<ref>PMID:35830796</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ujr" style="background-color:#fffaf0;"></div>

==See Also==
*[[Calcium/calmodulin dependent protein kinase 3D structures|Calcium/calmodulin dependent protein kinase 3D structures]]
*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Garman SC]]
[[Category: Ozden C]]
[[Category: Santos NJ]]
[[Category: Stratton MM]]