2n27

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(New page: '''Unreleased structure''' The entry 2n27 is ON HOLD Authors: Hetenyi, A., Nemeth, L., Weber, E., Szakonyi, G., Winter, Z., Josvay, K., Olah, Z., Martinek, T.A. Description: Direct att...)
Current revision (06:13, 15 May 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2n27 is ON HOLD
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==Competitive inhibition of TRPV1 calmodulin interaction by vanilloids==
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<StructureSection load='2n27' size='340' side='right'caption='[[2n27]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2n27]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N27 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4DY:(6E)-N-(4-HYDROXY-3-METHOXYBENZYL)-8-METHYLNON-6-ENAMIDE'>4DY</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n27 OCA], [https://pdbe.org/2n27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n27 RCSB], [https://www.ebi.ac.uk/pdbsum/2n27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n27 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4. The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of LQT14.
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== Function ==
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[https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).<ref>PMID:16760425</ref> <ref>PMID:23893133</ref> <ref>PMID:26969752</ref> <ref>PMID:27165696</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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There is enormous interest toward vanilloid agonists of the pain receptor TRPV1 in analgesic therapy, but the mechanisms of their sensory neuron-blocking effects at high or repeated doses are still a matter of debate. Our results have demonstrated that capsaicin and resiniferatoxin form nanomolar complexes with calmodulin, and competitively inhibit TRPV1-calmodulin interaction. These interactions involve the protein recognition interface of calmodulin, which is responsible for all of the cell-regulatory calmodulin-protein interactions. These results draw attention to a previously unknown vanilloid target, which may contribute to the explanation of the paradoxical pain-modulating behaviour of these important pharmacons. This article is protected by copyright. All rights reserved.
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Authors: Hetenyi, A., Nemeth, L., Weber, E., Szakonyi, G., Winter, Z., Josvay, K., Olah, Z., Martinek, T.A.
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Competitive inhibition of TRPV1 - calmodulin interaction by vanilloids.,Hetenyi A, Nemeth L, Weber E, Szakonyi G, Winter Z, Josvay K, Bartus E, Olah Z, Martinek TA FEBS Lett. 2016 Jun 24. doi: 10.1002/1873-3468.12267. PMID:27339229<ref>PMID:27339229</ref>
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Description: Direct attack of vanilloids on the regulation of the pain receptor TRPV1
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Martinek, T.A]]
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<div class="pdbe-citations 2n27" style="background-color:#fffaf0;"></div>
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[[Category: Weber, E]]
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== References ==
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[[Category: Josvay, K]]
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<references/>
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[[Category: Winter, Z]]
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__TOC__
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[[Category: Nemeth, L]]
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</StructureSection>
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[[Category: Szakonyi, G]]
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[[Category: Homo sapiens]]
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[[Category: Hetenyi, A]]
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[[Category: Large Structures]]
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[[Category: Olah, Z]]
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[[Category: Bartus E]]
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[[Category: Hetenyi A]]
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[[Category: Josvay K]]
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[[Category: Martinek TA]]
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[[Category: Nemeth L]]
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[[Category: Olah Z]]
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[[Category: Szakonyi G]]
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[[Category: Weber E]]
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[[Category: Winter Z]]

Current revision

Competitive inhibition of TRPV1 calmodulin interaction by vanilloids

PDB ID 2n27

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