Source:http://linkedlifedata.com/resource/pubmed/id/17214961
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2007-1-26
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pubmed:abstractText |
Calcium-permeable N-methyl-d-aspartate (NMDA) receptors are tetrameric cation channels composed of glycine-binding NR1 and glutamate-binding NR2 subunits, which require binding of both glutamate and glycine for efficient channel gating. In contrast, receptors assembled from NR1 and NR3 subunits function as calcium-impermeable excitatory glycine receptors that respond to agonist application only with low efficacy. Here, we show that antagonists of and substitutions within the glycine-binding site of NR1 potentiate NR1/NR3 receptor function up to 25-fold, but inhibition or mutation of the NR3 glycine binding site reduces or abolishes receptor activation. Thus, glycine bound to the NR1 subunit causes auto-inhibition of NR1/NR3 receptors whereas glycine binding to the NR3 subunits is required for opening of the ion channel. Our results establish differential roles of the high-affinity NR3 and low-affinity NR1 glycine-binding sites in excitatory glycine receptor function.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/NR1 NMDA receptor,
http://linkedlifedata.com/resource/pubmed/chemical/NR3A NMDA receptor,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, N-Methyl-D-Aspartate
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
354
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
102-8
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pubmed:meshHeading |
pubmed-meshheading:17214961-Animals,
pubmed-meshheading:17214961-Glycine,
pubmed-meshheading:17214961-Oocytes,
pubmed-meshheading:17214961-Protein Subunits,
pubmed-meshheading:17214961-Receptors, Glycine,
pubmed-meshheading:17214961-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:17214961-Structure-Activity Relationship,
pubmed-meshheading:17214961-Xenopus laevis
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pubmed:year |
2007
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pubmed:articleTitle |
Principal role of NR3 subunits in NR1/NR3 excitatory glycine receptor function.
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pubmed:affiliation |
Abteilung Neurochemie, Max-Planck-Institut für Hirnforschung, Deutschordenstr. 46, 60528 Frankfurt, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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