2jk4

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{{Seed}}
 
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[[Image:2jk4.png|left|200px]]
 
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==Structure of the human voltage-dependent anion channel==
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The line below this paragraph, containing "STRUCTURE_2jk4", creates the "Structure Box" on the page.
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<StructureSection load='2jk4' size='340' side='right'caption='[[2jk4]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2jk4]] 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=2JK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JK4 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.1&#8491;</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=2jk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jk4 OCA], [https://pdbe.org/2jk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jk4 RCSB], [https://www.ebi.ac.uk/pdbsum/2jk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jk4 ProSAT]</span></td></tr>
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{{STRUCTURE_2jk4| PDB=2jk4 | SCENE= }}
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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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jk/2jk4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jk4 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The voltage-dependent anion channel (VDAC), also known as mitochondrial porin, is the most abundant protein in the mitochondrial outer membrane (MOM). VDAC is the channel known to guide the metabolic flux across the MOM and plays a key role in mitochondrially induced apoptosis. Here, we present the 3D structure of human VDAC1, which was solved conjointly by NMR spectroscopy and x-ray crystallography. Human VDAC1 (hVDAC1) adopts a beta-barrel architecture composed of 19 beta-strands with an alpha-helix located horizontally midway within the pore. Bioinformatic analysis indicates that this channel architecture is common to all VDAC proteins and is adopted by the general import pore TOM40 of mammals, which is also located in the MOM.
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===STRUCTURE OF THE HUMAN VOLTAGE-DEPENDENT ANION CHANNEL===
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Structure of the human voltage-dependent anion channel.,Bayrhuber M, Meins T, Habeck M, Becker S, Giller K, Villinger S, Vonrhein C, Griesinger C, Zweckstetter M, Zeth K Proc Natl Acad Sci U S A. 2008 Oct 7;105(40):15370-5. Epub 2008 Oct 1. PMID:18832158<ref>PMID:18832158</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2jk4" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18832158}}, adds the Publication Abstract to the page
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18832158 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18832158}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2JK4 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JK4 OCA].
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==Reference==
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<ref group="xtra">PMID:18832158</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bayrhuber, M.]]
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[[Category: Large Structures]]
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[[Category: Becker, S.]]
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[[Category: Bayrhuber M]]
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[[Category: Giller, K.]]
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[[Category: Becker S]]
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[[Category: Griesinger, C.]]
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[[Category: Giller K]]
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[[Category: Habeck, M.]]
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[[Category: Griesinger C]]
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[[Category: Meins, T.]]
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[[Category: Habeck M]]
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[[Category: Villinger, S.]]
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[[Category: Meins T]]
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[[Category: Vonrhein, C.]]
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[[Category: Villinger S]]
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[[Category: Zeth, K.]]
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[[Category: Vonrhein C]]
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[[Category: Zweckstetter, M.]]
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[[Category: Zeth K]]
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[[Category: Acetylation]]
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[[Category: Zweckstetter M]]
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[[Category: Apoptosis]]
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[[Category: Cell membrane]]
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[[Category: Host-virus interaction]]
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[[Category: Ion transport]]
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[[Category: Membrane]]
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[[Category: Membrane protein]]
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[[Category: Mitochondrial outer membrane]]
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[[Category: Mitochondrion]]
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[[Category: Mitochondrion outer membrane]]
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[[Category: Phosphoprotein]]
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[[Category: Porin]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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[[Category: Vdac]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:01:02 2009''
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Current revision

Structure of the human voltage-dependent anion channel

PDB ID 2jk4

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