1ISR

Crystal Structure of Metabotropic Glutamate Receptor Subtype 1 Complexed with Glutamate and Gadolinium Ion

1ISR の概要

• エントリーDOI: 10.2210/pdb1isr/pdb
• 関連するPDBエントリー: 1EWK 1EWT 1EWV 1ISS
• 分子名称: Metabotropic Glutamate Receptor subtype 1, GLUTAMIC ACID, GADOLINIUM ATOM (3 entities in total)
• 機能のキーワード: signal transduction, neurotransmitter, g protein coupled receptor, agonist, gadolinium ion, signaling protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P23385
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55720.34

構造登録者

Tsuchiya, D.,Kunishima, N.,Kamiya, N.,Jingami, H.,Morikawa, K. (登録日: 2001-12-21, 公開日: 2002-03-13, 最終更新日: 2024-11-06)

主引用文献

Tsuchiya, D.,Kunishima, N.,Kamiya, N.,Jingami, H.,Morikawa, K.
Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd3+.
Proc.Natl.Acad.Sci.USA, 99:2660-2665, 2002

PubMed Abstract: Crystal structures of the extracellular ligand-binding region of the metabotropic glutamate receptor, complexed with an antagonist, (S)-(alpha)-methyl-4-carboxyphenylglycine, and with both glutamate and Gd3+ ion, have been determined by x-ray crystallographic analyses. The structure of the complex with the antagonist is similar to that of the unliganded resting dimer. The antagonist wedges the protomer to maintain an inactive open form. The glutamate/Gd3+ complex is an exact 2-fold symmetric dimer, where each bi-lobed protomer adopts the closed conformation. The surface of the C-terminal domain contains an acidic patch, whose negative charges are alleviated by the metal cation to stabilize the active dimeric structure. The structural comparison between the active and resting dimers suggests that glutamate binding tends to induce domain closing and a small shift of a helix in the dimer interface. Furthermore, an interprotomer contact including the acidic patch inhibited dimer formation by the two open protomers in the active state. These findings provide a structural basis to describe the link between ligand binding and the dimer interface.

PubMed: 11867751
DOI: 10.1073/pnas.052708599

実験手法

X-RAY DIFFRACTION (4 Å)