Source:http://linkedlifedata.com/resource/pubmed/id/11796999
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6869
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pubmed:dateCreated |
2002-1-17
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pubmed:databankReference | |
pubmed:abstractText |
The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. Genetic defects in ClC Cl- channels underlie several familial muscle and kidney diseases. Here we present the X-ray structures of two prokaryotic ClC Cl- channels from Salmonella enterica serovar typhimurium and Escherichia coli at 3.0 and 3.5 A, respectively. Both structures reveal two identical pores, each pore being formed by a separate subunit contained within a homodimeric membrane protein. Individual subunits are composed of two roughly repeated halves that span the membrane with opposite orientations. This antiparallel architecture defines a selectivity filter in which a Cl- ion is stabilized by electrostatic interactions with alpha-helix dipoles and by chemical coordination with nitrogen atoms and hydroxyl groups. These findings provide a structural basis for further understanding the function of ClC Cl- channels, and establish the physical and chemical basis of their anion selectivity.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anions,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chloride Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
415
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
287-94
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11796999-Amino Acid Sequence,
pubmed-meshheading:11796999-Animals,
pubmed-meshheading:11796999-Anions,
pubmed-meshheading:11796999-Bacterial Proteins,
pubmed-meshheading:11796999-Chloride Channels,
pubmed-meshheading:11796999-Crystallography, X-Ray,
pubmed-meshheading:11796999-Escherichia coli,
pubmed-meshheading:11796999-Escherichia coli Proteins,
pubmed-meshheading:11796999-Humans,
pubmed-meshheading:11796999-Ion Transport,
pubmed-meshheading:11796999-Models, Molecular,
pubmed-meshheading:11796999-Molecular Sequence Data,
pubmed-meshheading:11796999-Protein Conformation,
pubmed-meshheading:11796999-Recombinant Proteins,
pubmed-meshheading:11796999-Salmonella typhimurium,
pubmed-meshheading:11796999-Sequence Homology, Amino Acid
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pubmed:year |
2002
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pubmed:articleTitle |
X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity.
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pubmed:affiliation |
Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, Rockefeller University, 1230 York Avenue, New York, New York 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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