2MJ1

NMR structure of the soluble A beta 17-34 peptide

2MJ1 の概要

• エントリーDOI: 10.2210/pdb2mj1/pdb
• 関連するPDBエントリー: 1LFM
• NMR情報: BMRB: 19701
• 分子名称: Amyloid beta A4 protein (1 entity in total)
• 機能のキーワード: amyloid, alzheimer, hydrolase inhibitor
• 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: 1851.13

構造登録者

Fonar, G.,Samson, A.O. (登録日: 2013-12-23, 公開日: 2014-11-05, 最終更新日: 2024-05-15)

主引用文献

Fonar, G.,Samson, A.O.
NMR structure of the water soluble A beta 17-34 peptide.
Biosci.Rep., 34:e00155-e00155, 2014

PubMed Abstract: Alzheimer's disease is the most common neurodegenerative disorder in the world. Its most significant symptoms are memory loss and decrease in cognition. Alzheimer's disease is characterized by aggregation of two proteins in the brain namely Aβ (amyloid β) and tau. Recent evidence suggests that the interaction of soluble Aβ with nAChR (nicotinic acetylcholine receptors) contributes to disease progression. In this study, we determine the NMR structure of an Aβ17-34 peptide solubilized by the addition of two glutamic acids at each terminus. Our results indicate that the Aβ peptide adopts an α-helical structure for residues 19-26 and 28-33. The α-helical structure is broken around residues S26, N27 and K28, which form a kink in the helical conformation. This α-helix was not described earlier in an aqueous solution without organic solvents, and at physiological conditions (pH 7). These data are in agreement with Aβ adopting an α-helical conformation in the membrane before polymerizing into amyloid β-sheets and provide insight into the intermediate state of Aβ in Alzheimer's disease.

PubMed: 25284368
DOI: 10.1042/BSR20140094

実験手法

SOLUTION NMR