5jdp
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==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=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5jdp]] is a 1 chain structure. 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> | ||
| + | </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> | ||
| + | == 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> | ||
| + | <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> |
| + | <div class="pdbe-citations 5jdp" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Becker, S]] | ||
| + | [[Category: Giller, K]] | ||
| + | [[Category: Griesinger, C]] | ||
| + | [[Category: Jaremko, L]] | ||
| + | [[Category: Jaremko, M]] | ||
| + | [[Category: Schmidt, C]] | ||
| + | [[Category: Villinger, S]] | ||
| + | [[Category: Zweckstetter, M]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Protein dynamic]] | ||
| + | [[Category: Relaxation]] | ||
| + | [[Category: Sparse data]] | ||
| + | [[Category: Structure refinement]] | ||
Revision as of 16:05, 10 August 2016
E73V mutant of the human voltage-dependent anion channel
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