2fu3
From Proteopedia
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Crystal structure of gephyrin E-domain
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
2FU3 is a Single protein structure of sequence 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
Page seeded by OCA on Wed Nov 21 10:46:09 2007
