5jdp: Difference between revisions
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The | ==E73V mutant of the human voltage-dependent anion channel== | ||
<StructureSection load='5jdp' size='340' side='right'caption='[[5jdp]]' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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> | |||
</table> | |||
== Function == | |||
[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;"> | |||
== 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<ref>PMID:27461260</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5jdp" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Becker S]] | |||
[[Category: Giller K]] | |||
[[Category: Griesinger C]] | |||
[[Category: Jaremko L]] | |||
[[Category: Jaremko M]] | |||
[[Category: Schmidt C]] | |||
[[Category: Villinger S]] | |||
[[Category: Zweckstetter M]] | |||
