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New page: left|200px<br /><applet load="3bhh" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bhh, resolution 2.400Å" /> '''Crystal structure o... |
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== | ==Crystal structure of human calcium/calmodulin-dependent protein kinase IIB isoform 1 (CAMK2B)== | ||
<StructureSection load='3bhh' size='340' side='right'caption='[[3bhh]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
[[ | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3bhh]] is a 4 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=3BHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BHH 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]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5CP:[4-({4-[(5-CYCLOPROPYL-1H-PYRAZOL-3-YL)AMINO]-6-(METHYLAMINO)PYRIMIDIN-2-YL}AMINO)PHENYL]ACETONITRILE'>5CP</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=3bhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bhh OCA], [https://pdbe.org/3bhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bhh RCSB], [https://www.ebi.ac.uk/pdbsum/3bhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bhh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KCC2B_HUMAN KCC2B_HUMAN] Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle. In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Participates in the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2.<ref>PMID:16690701</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/bh/3bhh_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=3bhh ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[Calcium/calmodulin dependent protein kinase 3D structures|Calcium/calmodulin dependent protein kinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Arrowsmith | [[Category: Arrowsmith CH]] | ||
[[Category: Berridge | [[Category: Berridge G]] | ||
[[Category: Bullock | [[Category: Bullock A]] | ||
[[Category: Burgess | [[Category: Burgess N]] | ||
[[Category: Edwards AM]] | |||
[[Category: Edwards | [[Category: Filippakopoulos P]] | ||
[[Category: Filippakopoulos | [[Category: Knapp S]] | ||
[[Category: Knapp | [[Category: Niesen F]] | ||
[[Category: Niesen | [[Category: Pike ACW]] | ||
[[Category: Pike | [[Category: Pilka ES]] | ||
[[Category: Pilka | [[Category: Rellos P]] | ||
[[Category: Rellos | [[Category: Ugochukwu E]] | ||
[[Category: Weigelt J]] | |||
[[Category: Ugochukwu | [[Category: Von Delft F]] | ||
[[Category: Weigelt | |||
[[Category: | |||
Latest revision as of 15:08, 30 August 2023
Crystal structure of human calcium/calmodulin-dependent protein kinase IIB isoform 1 (CAMK2B)Crystal structure of human calcium/calmodulin-dependent protein kinase IIB isoform 1 (CAMK2B)
Structural highlights
FunctionKCC2B_HUMAN Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle. In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Participates in the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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