1EWK

CRYSTAL STRUCTURE OF METABOTROPIC GLUTAMATE RECEPTOR SUBTYPE 1 COMPLEXED WITH GLUTAMATE

1EWK の概要

• エントリーDOI: 10.2210/pdb1ewk/pdb
• 関連するPDBエントリー: 1EWT
• 分子名称: METABOTROPIC GLUTAMATE RECEPTOR SUBTYPE 1, 2-acetamido-2-deoxy-beta-D-glucopyranose, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: signal transduction, neurotransmitter, cns, neuron, signaling protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 112460.03

構造登録者

Kunishima, N.,Shimada, Y.,Jingami, H.,Morikawa, K. (登録日: 2000-04-26, 公開日: 2000-12-18, 最終更新日: 2024-10-16)

主引用文献

Kunishima, N.,Shimada, Y.,Tsuji, Y.,Sato, T.,Yamamoto, M.,Kumasaka, T.,Nakanishi, S.,Jingami, H.,Morikawa, K.
Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor.
Nature, 407:971-977, 2000

PubMed Abstract: The metabotropic glutamate receptors (mGluRs) are key receptors in the modulation of excitatory synaptic transmission in the central nervous system. Here we have determined three different crystal structures of the extracellular ligand-binding region of mGluR1--in a complex with glutamate and in two unliganded forms. They all showed disulphide-linked homodimers, whose 'active' and 'resting' conformations are modulated through the dimeric interface by a packed alpha-helical structure. The bi-lobed protomer architectures flexibly change their domain arrangements to form an 'open' or 'closed' conformation. The structures imply that glutamate binding stabilizes both the 'active' dimer and the 'closed' protomer in dynamic equilibrium. Movements of the four domains in the dimer are likely to affect the separation of the transmembrane and intracellular regions, and thereby activate the receptor. This scheme in the initial receptor activation could be applied generally to G-protein-coupled neurotransmitter receptors that possess extracellular ligand-binding sites.

PubMed: 11069170
DOI: 10.1038/35039564

実験手法

X-RAY DIFFRACTION (2.2 Å)