2FU3

Crystal structure of gephyrin E-domain

2FU3 の概要

• エントリーDOI: 10.2210/pdb2fu3/pdb
• 関連するPDBエントリー: 2FTS
• 分子名称: gephyrin (2 entities in total)
• 機能のキーワード: glycine receptor, gephyrin, neuroreceptor anchoring, biosynthetic protein-structural protein complex, biosynthetic protein/structural protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cell junction, synapse : Q03555
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91304.79

構造登録者

Kim, E.Y.,Schindelin, H. (登録日: 2006-01-25, 公開日: 2006-03-14, 最終更新日: 2024-02-14)

主引用文献

Kim, E.Y.,Schrader, N.,Smolinsky, B.,Bedet, C.,Vannier, C.,Schwarz, G.,Schindelin, H.
Deciphering the structural framework of glycine receptor anchoring by gephyrin.
Embo J., 25:1385-1395, 2006

PubMed Abstract: 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.

PubMed: 16511563
DOI: 10.1038/sj.emboj.7601029

実験手法

X-RAY DIFFRACTION (2.7 Å)