2fts: Difference between revisions

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{{STRUCTURE_2fts|  PDB=2fts  |  SCENE=  }}  
{{STRUCTURE_2fts|  PDB=2fts  |  SCENE=  }}  


'''Crystal structure of the glycine receptor-gephyrin complex'''
===Crystal structure of the glycine receptor-gephyrin complex===




==Overview==
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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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==About this Structure==
==About this Structure==
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[[Category: Glycine receptor]]
[[Category: Glycine receptor]]
[[Category: Neuroreceptor anchoring]]
[[Category: Neuroreceptor anchoring]]
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