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| | ==E73V mutant of the human voltage-dependent anion channel== | | ==E73V mutant of the human voltage-dependent anion channel== |
| - | <StructureSection load='5jdp' size='340' side='right'caption='[[5jdp]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='5jdp' size='340' side='right'caption='[[5jdp]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jdp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JDP FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VDAC1, VDAC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jdp OCA], [http://pdbe.org/5jdp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jdp RCSB], [http://www.ebi.ac.uk/pdbsum/5jdp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jdp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ion channels|Ion channels]] | + | *[[Ion channels 3D structures|Ion channels 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Becker, S]] | + | [[Category: Becker S]] |
| - | [[Category: Giller, K]] | + | [[Category: Giller K]] |
| - | [[Category: Griesinger, C]] | + | [[Category: Griesinger C]] |
| - | [[Category: Jaremko, L]] | + | [[Category: Jaremko L]] |
| - | [[Category: Jaremko, M]] | + | [[Category: Jaremko M]] |
| - | [[Category: Schmidt, C]] | + | [[Category: Schmidt C]] |
| - | [[Category: Villinger, S]] | + | [[Category: Villinger S]] |
| - | [[Category: Zweckstetter, M]] | + | [[Category: Zweckstetter M]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Protein dynamic]]
| + | |
| - | [[Category: Relaxation]]
| + | |
| - | [[Category: Sparse data]]
| + | |
| - | [[Category: Structure refinement]]
| + | |
| Structural highlights
Function
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.[1] [2] [3]
Publication Abstract from PubMed
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.
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Thinnes FP, Walter G, Hellmann KP, Hellmann T, Merker R, Kiafard Z, Eben-Brunnen J, Schwarzer C, Gotz H, Hilschmann N. Gadolinium as an opener of the outwardly rectifying Cl(-) channel (ORCC). Is there relevance for cystic fibrosis therapy? Pflugers Arch. 2001;443 Suppl 1:S111-6. Epub 2001 Jul 7. PMID:11845315 doi:http://dx.doi.org/10.1007/s004240100656
- ↑ Verrier F, Mignotte B, Jan G, Brenner C. Study of PTPC composition during apoptosis for identification of viral protein target. Ann N Y Acad Sci. 2003 Dec;1010:126-42. PMID:15033708
- ↑ Hiller S, Garces RG, Malia TJ, Orekhov VY, Colombini M, Wagner G. Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. Science. 2008 Aug 29;321(5893):1206-10. PMID:18755977 doi:321/5893/1206
- ↑ Jaremko M, Jaremko L, Villinger S, Schmidt CD, Griesinger C, Becker S, Zweckstetter M. High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins. Angew Chem Int Ed Engl. 2016 Jul 27. doi: 10.1002/anie.201602639. PMID:27461260 doi:http://dx.doi.org/10.1002/anie.201602639
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