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| ==Full-length human CaMKII== | | ==Full-length human CaMKII== |
- | <StructureSection load='3soa' size='340' side='right' caption='[[3soa]], [[Resolution|resolution]] 3.55Å' scene=''> | + | <StructureSection load='3soa' size='340' side='right'caption='[[3soa]], [[Resolution|resolution]] 3.55Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3soa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SOA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SOA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3soa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SOA FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DB8:4-[(2,4-DICHLORO-5-METHOXYPHENYL)AMINO]-6-METHOXY-7-[3-(4-METHYLPIPERAZIN-1-YL)PROPOXY]QUINOLINE-3-CARBONITRILE'>DB8</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5501Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">camk2a, camka, kiaa0968, camk2b, camkb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DB8:4-[(2,4-DICHLORO-5-METHOXYPHENYL)AMINO]-6-METHOXY-7-[3-(4-METHYLPIPERAZIN-1-YL)PROPOXY]QUINOLINE-3-CARBONITRILE'>DB8</scene></td></tr> |
- | <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>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3soa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3soa OCA], [https://pdbe.org/3soa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3soa RCSB], [https://www.ebi.ac.uk/pdbsum/3soa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3soa ProSAT]</span></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=3soa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3soa OCA], [http://pdbe.org/3soa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3soa RCSB], [http://www.ebi.ac.uk/pdbsum/3soa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3soa ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://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). | + | [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;">
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- | == Publication Abstract from PubMed ==
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- | Calcium/calmodulin-dependent kinase II (CaMKII) forms a highly conserved dodecameric assembly that is sensitive to the frequency of calcium pulse trains. Neither the structure of the dodecameric assembly nor how it regulates CaMKII are known. We present the crystal structure of an autoinhibited full-length human CaMKII holoenzyme, revealing an unexpected compact arrangement of kinase domains docked against a central hub, with the calmodulin-binding sites completely inaccessible. We show that this compact docking is important for the autoinhibition of the kinase domains and for setting the calcium response of the holoenzyme. Comparison of CaMKII isoforms, which differ in the length of the linker between the kinase domain and the hub, demonstrates that these interactions can be strengthened or weakened by changes in linker length. This equilibrium between autoinhibited states provides a simple mechanism for tuning the calcium response without changes in either the hub or the kinase domains. PAPERFLICK:
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- | A Mechanism for Tunable Autoinhibition in the Structure of a Human Ca(2+)/Calmodulin- Dependent Kinase II Holoenzyme.,Chao LH, Stratton MM, Lee IH, Rosenberg OS, Levitz J, Mandell DJ, Kortemme T, Groves JT, Schulman H, Kuriyan J Cell. 2011 Sep 2;146(5):732-45. PMID:21884935<ref>PMID:21884935</ref>
| + | ==See Also== |
- | | + | *[[Calcium/calmodulin dependent protein kinase 3D structures|Calcium/calmodulin dependent protein kinase 3D structures]] |
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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- | </div>
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- | <div class="pdbe-citations 3soa" style="background-color:#fffaf0;"></div>
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- | == References ==
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- | <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Calcium/calmodulin-dependent protein kinase]] | + | [[Category: Homo sapiens]] |
- | [[Category: Human]] | + | [[Category: Large Structures]] |
- | [[Category: Chao, L H]] | + | [[Category: Chao LH]] |
- | [[Category: Kuriyan, J]] | + | [[Category: Kuriyan J]] |
- | [[Category: Calcium/calmodulin]]
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- | [[Category: Cytosolic]]
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- | [[Category: Kinase]]
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- | [[Category: Phosphorylation]]
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- | [[Category: Protein kinase]]
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- | [[Category: Transferase-transferase inhibitor complex]]
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