2fts
From Proteopedia
(New page: 200px<br /><applet load="2fts" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fts, resolution 2.410Å" /> '''Crystal structure o...) |
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| - | [[Image:2fts.gif|left|200px]]<br /><applet load="2fts" size=" | + | [[Image:2fts.gif|left|200px]]<br /><applet load="2fts" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fts, resolution 2.410Å" /> | caption="2fts, resolution 2.410Å" /> | ||
'''Crystal structure of the glycine receptor-gephyrin complex'''<br /> | '''Crystal structure of the glycine receptor-gephyrin complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Glycine is the major inhibitory neurotransmitter in the spinal cord and | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2FTS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 2FTS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FTS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: Kim, E | + | [[Category: Kim, E Y.]] |
[[Category: Schindelin, H.]] | [[Category: Schindelin, H.]] | ||
[[Category: gephyrin]] | [[Category: gephyrin]] | ||
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[[Category: neuroreceptor anchoring]] | [[Category: neuroreceptor anchoring]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:25:04 2008'' |
Revision as of 15:25, 21 February 2008
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Crystal structure of the glycine receptor-gephyrin complex
Overview
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.
About this Structure
2FTS is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Deciphering the structural framework of glycine receptor anchoring by gephyrin., Kim EY, Schrader N, Smolinsky B, Bedet C, Vannier C, Schwarz G, Schindelin H, EMBO J. 2006 Mar 22;25(6):1385-95. Epub 2006 Mar 2. PMID:16511563
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