2jk4: Difference between revisions
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<StructureSection load='2jk4' size='340' side='right'caption='[[2jk4]], [[Resolution|resolution]] 4.10Å' scene=''> | <StructureSection load='2jk4' size='340' side='right'caption='[[2jk4]], [[Resolution|resolution]] 4.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jk4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2jk4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=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> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 11:13, 19 January 2022
Structure of the human voltage-dependent anion channelStructure of the human voltage-dependent anion channel
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Human
- Large Structures
- Bayrhuber, M
- Becker, S
- Giller, K
- Griesinger, C
- Habeck, M
- Meins, T
- Villinger, S
- Vonrhein, C
- Zeth, K
- Zweckstetter, M
- Acetylation
- Apoptosis
- Cell membrane
- Host-virus interaction
- Ion transport
- Membrane
- Membrane protein
- Mitochondrial outer membrane
- Mitochondrion
- Mitochondrion outer membrane
- Phosphoprotein
- Porin
- Transmembrane
- Transport
- Vdac