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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
46
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pubmed:dateCreated |
2008-11-21
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pubmed:databankReference |
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pubmed:abstractText |
The voltage-dependent anion channel (VDAC) constitutes the major pathway for the entry and exit of metabolites across the outer membrane of the mitochondria and can serve as a scaffold for molecules that modulate the organelle. We report the crystal structure of a beta-barrel eukaryotic membrane protein, the murine VDAC1 (mVDAC1) at 2.3 A resolution, revealing a high-resolution image of its architecture formed by 19 beta-strands. Unlike the recent NMR structure of human VDAC1, the position of the voltage-sensing N-terminal segment is clearly resolved. The alpha-helix of the N-terminal segment is oriented against the interior wall, causing a partial narrowing at the center of the pore. This segment is ideally positioned to regulate the conductance of ions and metabolites passing through the VDAC pore.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-1011248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-10365962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-11829498,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-12044860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-12393927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-12881569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-12893935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-12933700,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-14646133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-15572765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-15607740,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-15818409,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-16285865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-16307870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-16354668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-16597621,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-16930689,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-1718414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-17328803,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-17336328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-17387661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-17439818,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-17828567,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-18469866,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-2482359,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-3008816,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-3214181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-450112,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-6215413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-7542652,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-7685355,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-7685903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-8744209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-9593723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-9733730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18988731-9757107
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1091-6490
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
18
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17742-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:18988731-Animals,
pubmed-meshheading:18988731-Crystallography, X-Ray,
pubmed-meshheading:18988731-Ion Channel Gating,
pubmed-meshheading:18988731-Mice,
pubmed-meshheading:18988731-Models, Molecular,
pubmed-meshheading:18988731-Porosity,
pubmed-meshheading:18988731-Protein Structure, Secondary,
pubmed-meshheading:18988731-Protein Structure, Tertiary,
pubmed-meshheading:18988731-Solubility,
pubmed-meshheading:18988731-Static Electricity,
pubmed-meshheading:18988731-Voltage-Dependent Anion Channel 1
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pubmed:year |
2008
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pubmed:articleTitle |
The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating.
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pubmed:affiliation |
Department of Physiology, Cardiovascular Research Laboratories, David Geffen School of Medicine, University of California, Los Angeles, CA 90095, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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