3QLT

Crystal structure of a GluK2 (GluR6) glycan wedge homodimer assembly

3QLT の概要

• エントリーDOI: 10.2210/pdb3qlt/pdb
• 関連するPDBエントリー: 3H6G 3OLZ 3OM0 3QLU 3QLV
• 分子名称: Glutamate receptor, ionotropic kainate 2, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: membrane protein, glycosylation
• 由来する生物種: Rattus norvegicus (rat)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90973.59

構造登録者

Kumar, J.,Mayer, M.L. (登録日: 2011-02-03, 公開日: 2011-08-03, 最終更新日: 2024-11-06)

主引用文献

Kumar, J.,Schuck, P.,Mayer, M.L.
Structure and assembly mechanism for heteromeric kainate receptors.
Neuron, 71:319-331, 2011

PubMed Abstract: Native glutamate receptor ion channels are tetrameric assemblies containing two or more different subunits. NMDA receptors are obligate heteromers formed by coassembly of two or three divergent gene families. While some AMPA and kainate receptors can form functional homomeric ion channels, the KA1 and KA2 subunits are obligate heteromers which function only in combination with GluR5-7. The mechanisms controlling glutamate receptor assembly involve an initial step in which the amino terminal domains (ATD) assemble as dimers. Here, we establish by sedimentation velocity that the ATDs of GluR6 and KA2 coassemble as a heterodimer of K(d) 11 nM, 32,000-fold lower than the K(d) for homodimer formation by KA2; we solve crystal structures for the GluR6/KA2 ATD heterodimer and heterotetramer assemblies. Using these structures as a guide, we perform a mutant cycle analysis to probe the energetics of assembly and show that high-affinity ATD interactions are required for biosynthesis of functional heteromeric receptors.

PubMed: 21791290
DOI: 10.1016/j.neuron.2011.05.038

実験手法

X-RAY DIFFRACTION (2.988 Å)