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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 |
2010-11-18
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pubmed:abstractText |
Nerve signaling in humans and chemical sensing in bacteria both rely on the controlled opening and closing of the ion-conducting pore in pentameric ligand-gated ion channels. With the help of a multiscale simulation approach that combines mixed elastic network model calculations with molecular dynamics simulations, we study the opening and closing of the pore in Gloeobacter violaceus channel GLIC at atomic resolution. In our simulations of the GLIC transmembrane domain, we first verify that the two endpoints of the transition are open and closed to sodium ion conduction, respectively. We then show that a two-stage tilting of the pore-lining helices induces cooperative drying and iris-like closing of the channel pore. From the free energy profile of the gating transition and from unrestrained simulations, we conclude that the pore of the isolated GLIC transmembrane domain closes spontaneously. The mechanical work of opening the pore is performed primarily on the M2-M3 loop. Strong interactions of this short and conserved loop with the extracellular domain are therefore crucial to couple ligand binding to channel opening.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-10962011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-11700553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-12023216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-15111405,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-15701510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-15805177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-15837197,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-16500984,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-16554804,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-16829701,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-16844753,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-17726097,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-18768796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-18987630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-18987633,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-19450479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-19486673,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21041674-9195488
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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 |
16
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pubmed:volume |
107
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
19814-9
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pubmed:dateRevised |
2011-7-28
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pubmed:meshHeading |
pubmed-meshheading:21041674-Bacterial Proteins,
pubmed-meshheading:21041674-Computer Simulation,
pubmed-meshheading:21041674-Cyanobacteria,
pubmed-meshheading:21041674-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:21041674-Ion Channel Gating,
pubmed-meshheading:21041674-Kinetics,
pubmed-meshheading:21041674-Ligand-Gated Ion Channels,
pubmed-meshheading:21041674-Models, Molecular,
pubmed-meshheading:21041674-Protein Structure, Quaternary,
pubmed-meshheading:21041674-Protein Structure, Secondary,
pubmed-meshheading:21041674-Protein Structure, Tertiary,
pubmed-meshheading:21041674-Thermodynamics,
pubmed-meshheading:21041674-Time Factors
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pubmed:year |
2010
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pubmed:articleTitle |
Pore opening and closing of a pentameric ligand-gated ion channel.
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pubmed:affiliation |
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Intramural
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