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5jdp

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'''Unreleased structure'''
 
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The entry 5jdp is ON HOLD
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==E73V mutant of the human voltage-dependent anion channel==
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<StructureSection load='5jdp' size='340' side='right'caption='[[5jdp]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5jdp]] 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=5JDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JDP FirstGlance]. <br>
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</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=5jdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jdp OCA], [https://pdbe.org/5jdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jdp RCSB], [https://www.ebi.ac.uk/pdbsum/5jdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jdp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VDAC1_HUMAN VDAC1_HUMAN] Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.<ref>PMID:11845315</ref> <ref>PMID:15033708</ref> <ref>PMID:18755977</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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15 N spin-relaxation rates are demonstrated to provide critical information about the long-range structure and internal motions of membrane proteins. Combined with an improved calculation method, the relaxation-rate-derived structure of the 283-residue human voltage-dependent anion channel revealed an anisotropically shaped barrel with a rigidly attached N-terminal helix. Our study thus establishes an NMR spectroscopic approach to determine the structure and dynamics of mammalian membrane proteins at high accuracy and resolution.
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Authors:
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High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins.,Jaremko M, Jaremko L, Villinger S, Schmidt CD, Griesinger C, Becker S, Zweckstetter M Angew Chem Int Ed Engl. 2016 Jul 27. doi: 10.1002/anie.201602639. PMID:27461260<ref>PMID:27461260</ref>
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Description:
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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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<div class="pdbe-citations 5jdp" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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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: Becker S]]
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[[Category: Giller K]]
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[[Category: Griesinger C]]
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[[Category: Jaremko L]]
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[[Category: Jaremko M]]
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[[Category: Schmidt C]]
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[[Category: Villinger S]]
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[[Category: Zweckstetter M]]

Current revision

E73V mutant of the human voltage-dependent anion channel

PDB ID 5jdp

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