2M9S

3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside

2M9S の概要

• エントリーDOI: 10.2210/pdb2m9s/pdb
• 関連するPDBエントリー: 2M9R
• 分子名称: Amyloid beta A4 protein, (2S,3S)-3-(3,5-dihydroxyphenyl)-2-(4-hydroxyphenyl)-4-[(E)-2-(4-hydroxyphenyl)ethenyl]-2,3-dihydro-1-benzofuran-6-yl beta-D-glucopyranoside (2 entities in total)
• 機能のキーワード: amyloid peptide, protein fibril
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P05067
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5569.07

構造登録者

Monti, J.,Richard, T. (登録日: 2013-06-19, 公開日: 2013-09-11, 最終更新日: 2024-05-01)

主引用文献

Richard, T.,Papastamoulis, Y.,Pierre, W.T.,Monti, J.P.
3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside: Implications in Alzheimer's disease.
Biochim.Biophys.Acta, 1830:5068-5074, 2013

PubMed Abstract: Alzheimer's disease (AD) is a progressive neurodegenerative disorder. There is a consensus that Aβ is a pathologic agent and that its toxic effects, which are at present incompletely understood, may occur through several potential mechanisms. Polyphenols are known to have wide-ranging properties with regard to health and for helping to prevent various diseases like neurodegenerative disorders. Thus inhibiting the formation of toxic Aβ assemblies is a reasonable hypothesis to prevent and perhaps treat AD METHODS: Solution NMR and molecular modeling were used to obtain more information about the interaction between the Aβ1-40 and the polyphenol ε-viniferin glucoside (EVG) and particularly the Aβ residues involved in the complex.

PubMed: 23830862
DOI: 10.1016/j.bbagen.2013.06.031

実験手法

SOLUTION NMR