8uq2

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(Replacing page with ''''Unreleased structure''' The entry 8uq2 is ON HOLD Authors: Miotto, M.C., Marks, A.R. Description: Structure of human RyR2-S2808D in the subprimed state [[Category: Unrel...')
Current revision (05:28, 25 September 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8uq2 is ON HOLD
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==Structure of human RyR2-S2808D in the subprimed state==
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<StructureSection load='8uq2' size='340' side='right'caption='[[8uq2]], [[Resolution|resolution]] 2.98&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8uq2]] is a 8 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=8UQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8UQ2 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">Electron Microscopy, [[Resolution|Resolution]] 2.98&#8491;</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=8uq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8uq2 OCA], [https://pdbe.org/8uq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8uq2 RCSB], [https://www.ebi.ac.uk/pdbsum/8uq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8uq2 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/RYR2_HUMAN RYR2_HUMAN] Familial isolated arrhythmogenic ventricular dysplasia, right dominant form;Catecholaminergic polymorphic ventricular tachycardia;Familial isolated arrhythmogenic ventricular dysplasia, biventricular form;Familial isolated arrhythmogenic ventricular dysplasia, left dominant form. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/RYR2_HUMAN RYR2_HUMAN] Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity is modulated by formation of heterotetramers with RYR3. Required for cellular calcium ion homeostasis. Required for embryonic heart development.<ref>PMID:10830164</ref> <ref>PMID:20056922</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Heart failure, the leading cause of mortality and morbidity in the developed world, is characterized by cardiac ryanodine receptor 2 channels that are hyperphosphorylated, oxidized, and depleted of the stabilizing subunit calstabin-2. This results in a diastolic sarcoplasmic reticulum Ca(2+) leak that impairs cardiac contractility and triggers arrhythmias. Genetic mutations in ryanodine receptor 2 can also cause Ca(2+) leak, leading to arrhythmias and sudden cardiac death. Here, we solved the cryogenic electron microscopy structures of ryanodine receptor 2 variants linked either to heart failure or inherited sudden cardiac death. All are in the primed state, part way between closed and open. Binding of Rycal drugs to ryanodine receptor 2 channels reverts the primed state back towards the closed state, decreasing Ca(2+) leak, improving cardiac function, and preventing arrhythmias. We propose a structural-physiological mechanism whereby the ryanodine receptor 2 channel primed state underlies the arrhythmias in heart failure and arrhythmogenic disorders.
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Authors: Miotto, M.C., Marks, A.R.
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Structural basis for ryanodine receptor type 2 leak in heart failure and arrhythmogenic disorders.,Miotto MC, Reiken S, Wronska A, Yuan Q, Dridi H, Liu Y, Weninger G, Tchagou C, Marks AR Nat Commun. 2024 Sep 15;15(1):8080. doi: 10.1038/s41467-024-51791-y. PMID:39278969<ref>PMID:39278969</ref>
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Description: Structure of human RyR2-S2808D in the subprimed state
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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: Miotto, M.C]]
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<div class="pdbe-citations 8uq2" style="background-color:#fffaf0;"></div>
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[[Category: Marks, A.R]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Marks AR]]
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[[Category: Miotto MC]]

Current revision

Structure of human RyR2-S2808D in the subprimed state

PDB ID 8uq2

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