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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2006-3-22
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pubmed:databankReference |
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pubmed:abstractText |
Glycine is the major inhibitory neurotransmitter in the spinal cord and brain stem. Gephyrin is required to achieve a high concentration of glycine receptors (GlyRs) in the postsynaptic membrane, which is crucial for efficient glycinergic signal transduction. The interaction between gephyrin and the GlyR involves the E-domain of gephyrin and a cytoplasmic loop located between transmembrane segments three and four of the GlyR beta subunit. Here, we present crystal structures of the gephyrin E-domain with and without the GlyR beta-loop at 2.4 and 2.7 A resolutions, respectively. The GlyR beta-loop is bound in a symmetric 'key and lock' fashion to each E-domain monomer in a pocket adjacent to the dimer interface. Structure-guided mutagenesis followed by in vitro binding and in vivo colocalization assays demonstrate that a hydrophobic interaction formed by Phe 330 of gephyrin and Phe 398 and Ile 400 of the GlyR beta-loop is crucial for binding.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-10037506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-10325225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-10331874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-10581970,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-10607391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-10636880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-10845110,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-10900017,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-10941193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-11083919,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-11092928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-11095995,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-11283747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-11437237,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-11554796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-12097491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-12351820,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-12684523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-12967995,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-1319186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-14976213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-14993666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-15201864,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-15383648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-15748848,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-1657993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-3032237,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-6286620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-8264797,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-8581315,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-8745398,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-9379923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-9732459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-9757107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-9812897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16511563-9990024
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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 |
Mar
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1385-95
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16511563-Amino Acid Sequence,
pubmed-meshheading:16511563-Carrier Proteins,
pubmed-meshheading:16511563-Crystallography, X-Ray,
pubmed-meshheading:16511563-Humans,
pubmed-meshheading:16511563-Membrane Proteins,
pubmed-meshheading:16511563-Models, Molecular,
pubmed-meshheading:16511563-Molecular Sequence Data,
pubmed-meshheading:16511563-Mutagenesis, Site-Directed,
pubmed-meshheading:16511563-Protein Binding,
pubmed-meshheading:16511563-Protein Structure, Tertiary,
pubmed-meshheading:16511563-Receptors, Glycine,
pubmed-meshheading:16511563-Recombinant Proteins,
pubmed-meshheading:16511563-Sequence Homology, Amino Acid,
pubmed-meshheading:16511563-Signal Transduction,
pubmed-meshheading:16511563-Synapses
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pubmed:year |
2006
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pubmed:articleTitle |
Deciphering the structural framework of glycine receptor anchoring by gephyrin.
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pubmed:affiliation |
Department of Biochemistry, Center for Structural Biology, State University of New York, Stony Brook, NY 11794-5115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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