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| - | [[Image:1hkx.gif|left|200px]] | |
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| - | <!-- | + | ==Crystal structure of calcium/calmodulin-dependent protein kinase== |
| - | The line below this paragraph, containing "STRUCTURE_1hkx", creates the "Structure Box" on the page.
| + | <StructureSection load='1hkx' size='340' side='right'caption='[[1hkx]], [[Resolution|resolution]] 2.65Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1hkx]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HKX FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65Å</td></tr> |
| - | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=TBR:HEXATANTALUM+DODECABROMIDE'>TBR</scene></td></tr> |
| - | {{STRUCTURE_1hkx| PDB=1hkx | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hkx OCA], [https://pdbe.org/1hkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hkx RCSB], [https://www.ebi.ac.uk/pdbsum/1hkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hkx ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/KCC2A_MOUSE KCC2A_MOUSE] Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in various processes, such as synaptic plasticity, neurotransmitter release and long-term potentiation (By similarity). Member of the NMDAR signaling complex in excitatory synapses, it regulates NMDAR-dependent potentiation of the AMPAR and therefore excitatory synaptic transmission (By similarity). Regulates dendritic spine development (By similarity). Also regulates the migration of developing neurons (By similarity). Phosphorylates the transcription factor FOXO3 to activate its transcriptional activity (PubMed:23805378). Phosphorylates the transcription factor ETS1 in response to calcium signaling, thereby decreasing ETS1 affinity for DNA (PubMed:15994560). In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity). In response to interferon-beta (IFN-beta) stimulation, stimulates the JAK-STAT signaling pathway (By similarity). Acts as a negative regulator of 2-arachidonoylglycerol (2-AG)-mediated synaptic signaling via modulation of DAGLA activity (PubMed:23502535).[UniProtKB:P11275][UniProtKB:Q9UQM7]<ref>PMID:15994560</ref> <ref>PMID:23502535</ref> <ref>PMID:23805378</ref> Has no kinase activity.<ref>PMID:8524307</ref> |
| | + | == 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/hk/1hkx_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/main_output.php?pdb_ID=1hkx ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | We report the crystal structure of the 143 residue association domain of Ca(2+)/calmodulin-dependent protein kinase II (CaMKII). The association domain forms a hub-like assembly, composed of two rings of seven protomers each, which are stacked head to head and held together by extensive interfaces. The tetradecameric organization of the assembly was confirmed by analytical ultracentrifugation and multiangle light scattering. Individual protomers form wedge-shaped structures from which N-terminal helical segments that connect to the kinase domain extend toward the equatorial plane of the assembly, consistent with the arrangement of the kinase domains in a second outer ring. A deep and highly conserved pocket present within the association domain may serve as a docking site for proteins that interact with CaMKII. |
| | | | |
| - | '''CRYSTAL STRUCTURE OF CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE'''
| + | Crystal structure of a tetradecameric assembly of the association domain of Ca2+/calmodulin-dependent kinase II.,Hoelz A, Nairn AC, Kuriyan J Mol Cell. 2003 May;11(5):1241-51. PMID:12769848<ref>PMID:12769848</ref> |
| - | | + | |
| - | | + | |
| - | ==Overview==
| + | |
| - | We report the crystal structure of the 143 residue association domain of Ca(2+)/calmodulin-dependent protein kinase II (CaMKII). The association domain forms a hub-like assembly, composed of two rings of seven protomers each, which are stacked head to head and held together by extensive interfaces. The tetradecameric organization of the assembly was confirmed by analytical ultracentrifugation and multiangle light scattering. Individual protomers form wedge-shaped structures from which N-terminal helical segments that connect to the kinase domain extend toward the equatorial plane of the assembly, consistent with the arrangement of the kinase domains in a second outer ring. A deep and highly conserved pocket present within the association domain may serve as a docking site for proteins that interact with CaMKII.
| + | |
| | | | |
| - | ==About this Structure==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | 1HKX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HKX OCA].
| + | </div> |
| | + | <div class="pdbe-citations 1hkx" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Reference== | + | ==See Also== |
| - | Crystal structure of a tetradecameric assembly of the association domain of Ca2+/calmodulin-dependent kinase II., Hoelz A, Nairn AC, Kuriyan J, Mol Cell. 2003 May;11(5):1241-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12769848 12769848]
| + | *[[Calcium/calmodulin dependent protein kinase 3D structures|Calcium/calmodulin dependent protein kinase 3D structures]] |
| - | [[Category: Calcium/calmodulin-dependent protein kinase]] | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Single protein]]
| + | [[Category: Hoelz A]] |
| - | [[Category: Hoelz, A.]] | + | [[Category: Kuriyan J]] |
| - | [[Category: Kuriyan, J.]] | + | [[Category: Nairn AC]] |
| - | [[Category: Nairn, A C.]] | + | |
| - | [[Category: Alternative splicing]]
| + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Calmodulin-binding]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Serine/threonine-protein kinase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:57:42 2008''
| + | |
| Structural highlights
Function
KCC2A_MOUSE Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in various processes, such as synaptic plasticity, neurotransmitter release and long-term potentiation (By similarity). Member of the NMDAR signaling complex in excitatory synapses, it regulates NMDAR-dependent potentiation of the AMPAR and therefore excitatory synaptic transmission (By similarity). Regulates dendritic spine development (By similarity). Also regulates the migration of developing neurons (By similarity). Phosphorylates the transcription factor FOXO3 to activate its transcriptional activity (PubMed:23805378). Phosphorylates the transcription factor ETS1 in response to calcium signaling, thereby decreasing ETS1 affinity for DNA (PubMed:15994560). In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity). In response to interferon-beta (IFN-beta) stimulation, stimulates the JAK-STAT signaling pathway (By similarity). Acts as a negative regulator of 2-arachidonoylglycerol (2-AG)-mediated synaptic signaling via modulation of DAGLA activity (PubMed:23502535).[UniProtKB:P11275][UniProtKB:Q9UQM7][1] [2] [3] Has no kinase activity.[4]
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 PubMed
We report the crystal structure of the 143 residue association domain of Ca(2+)/calmodulin-dependent protein kinase II (CaMKII). The association domain forms a hub-like assembly, composed of two rings of seven protomers each, which are stacked head to head and held together by extensive interfaces. The tetradecameric organization of the assembly was confirmed by analytical ultracentrifugation and multiangle light scattering. Individual protomers form wedge-shaped structures from which N-terminal helical segments that connect to the kinase domain extend toward the equatorial plane of the assembly, consistent with the arrangement of the kinase domains in a second outer ring. A deep and highly conserved pocket present within the association domain may serve as a docking site for proteins that interact with CaMKII.
Crystal structure of a tetradecameric assembly of the association domain of Ca2+/calmodulin-dependent kinase II.,Hoelz A, Nairn AC, Kuriyan J Mol Cell. 2003 May;11(5):1241-51. PMID:12769848[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pufall MA, Lee GM, Nelson ML, Kang HS, Velyvis A, Kay LE, McIntosh LP, Graves BJ. Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region. Science. 2005 Jul 1;309(5731):142-5. doi: 10.1126/science.1111915. PMID:15994560 doi:http://dx.doi.org/10.1126/science.1111915
- ↑ Shonesy BC, Wang X, Rose KL, Ramikie TS, Cavener VS, Rentz T, Baucum AJ 2nd, Jalan-Sakrikar N, Mackie K, Winder DG, Patel S, Colbran RJ. CaMKII regulates diacylglycerol lipase-alpha and striatal endocannabinoid signaling. Nat Neurosci. 2013 Apr;16(4):456-63. doi: 10.1038/nn.3353. Epub 2013 Mar 17. PMID:23502535 doi:http://dx.doi.org/10.1038/nn.3353
- ↑ Tao L, Xie Q, Ding YH, Li ST, Peng S, Zhang YP, Tan D, Yuan Z, Dong MQ. CAMKII and Calcineurin regulate the lifespan of Caenorhabditis elegans through the FOXO transcription factor DAF-16. Elife. 2013 Jun 25;2:e00518. doi: 10.7554/eLife.00518. PMID:23805378 doi:http://dx.doi.org/10.7554/eLife.00518
- ↑ Bayer KU, Lohler J, Harbers K. An alternative, nonkinase product of the brain-specifically expressed Ca2+/calmodulin-dependent kinase II alpha isoform gene in skeletal muscle. Mol Cell Biol. 1996 Jan;16(1):29-36. PMID:8524307
- ↑ Hoelz A, Nairn AC, Kuriyan J. Crystal structure of a tetradecameric assembly of the association domain of Ca2+/calmodulin-dependent kinase II. Mol Cell. 2003 May;11(5):1241-51. PMID:12769848
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