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8qcy

From Proteopedia

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(New page: '''Unreleased structure''' The entry 8qcy is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (05:28, 17 April 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8qcy is ON HOLD
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==Cryo-EM structure of the outward-facing FLVCR2==
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<StructureSection load='8qcy' size='340' side='right'caption='[[8qcy]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8qcy]] is a 1 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=8QCY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QCY FirstGlance]. <br>
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Description:
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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]] 2.9&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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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=8qcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qcy OCA], [https://pdbe.org/8qcy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qcy RCSB], [https://www.ebi.ac.uk/pdbsum/8qcy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qcy ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/FLVC2_HUMAN FLVC2_HUMAN] Fowler vasculopathy. The disease is caused by variants affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/FLVC2_HUMAN FLVC2_HUMAN] Putative heme b importer/sensor involved in heme homeostasis in response to the metabolic state of the cell and to diet. May act as a sensor of cytosolic and/or mitochondrial heme levels to regulate mitochondrial respiration processes, ATP synthesis and thermogenesis. At low heme levels, interacts with components of electron transfer chain (ETC) complexes and ATP2A2, leading to ubiquitin-mediated degradation of ATP2A2 and inhibition of thermogenesis. Upon heme binding, dissociates from ETC complexes to allow switching from mitochondrial ATP synthesis to thermogenesis. Alternatively, in coordination with ATP2A2 may mediate calcium transport and signaling in response to heme.<ref>PMID:20823265</ref> <ref>PMID:32973183</ref>
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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: Safarian S]]
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[[Category: Weng T-H]]
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[[Category: Wu D]]

Current revision

Cryo-EM structure of the outward-facing FLVCR2

PDB ID 8qcy

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