6m7h: Difference between revisions

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-'''Unreleased structure'''
-The entry 6m7h is ON HOLD  until Paper Publication
+==Structure of calmodulin with KN93==
+<StructureSection load='6m7h' size='340' side='right'caption='[[6m7h]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6m7h]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M7H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6M7H FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=KN9:N-[2-[[[3-(4-Chlorophenyl)-2-propenyl]methylamino]methyl]phenyl]-N-(2-hydroxyethyl)-4-methoxybenzenesulfonamide'>KN9</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=6m7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m7h OCA], [http://pdbe.org/6m7h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m7h RCSB], [http://www.ebi.ac.uk/pdbsum/6m7h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m7h ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Here we report the structure of the widely utilized calmodulin (CaM)-dependent protein kinase II (CaMKII) inhibitor KN93 bound to the Ca(2+)-sensing protein CaM. KN93 is widely believed to inhibit CaMKII by binding to the kinase. The CaM-KN93 interaction is significant as it can interfere with the interaction between CaM and it's physiological targets, thereby raising the possibility of ascribing modified protein function to CaMKII phosphorylation while concealing a CaM-protein interaction. NMR spectroscopy, stopped-flow kinetic measurements, and x-ray crystallography were used to characterize the structure and biophysical properties of the CaM-KN93 interaction. We then investigated the functional properties of the cardiac Na(+) channel (NaV1.5) and ryanodine receptor (RyR2). We find that KN93 disrupts a high affinity CaM-NaV1.5 interaction and alters channel function independent of CaMKII. Moreover, KN93 increases RyR2 Ca(2+) release in cardiomyocytes independent of CaMKII. Therefore, when interpreting KN93 data, targets other than CaMKII need to be considered.
-Authors: Damo, S.M., Pattanayek, R.
+The CaMKII inhibitor KN93-calmodulin interaction and implications for calmodulin tuning of NaV1.5 and RyR2 function.,Johnson CN, Pattanayek R, Potet F, Rebbeck RT, Blackwell DJ, Nikolaienko R, Sequeira V, Le Meur R, Radwanski PB, Davis JP, Zima AV, Cornea RL, Damo SM, Gyorke S, George AL Jr, Knollmann BC Cell Calcium. 2019 Sep;82:102063. doi: 10.1016/j.ceca.2019.102063. Epub 2019 Jul , 30. PMID:31401388<ref>PMID:31401388</ref>
-Description: Structure of calmodulin with KN93
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6m7h" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Damo, S M]]
 [[Category: Pattanayek, R]]
-[[Category: Damo, S.M]]
+[[Category: Ca2+ binding ef-hand inhibitor complex]]
+[[Category: Signaling protein]]