2LFM

A partially folded structure of amyloid-beta(1 40) in an aqueous environment

2LFM の概要

• エントリーDOI: 10.2210/pdb2lfm/pdb
• NMR情報: BMRB: 17764
• 分子名称: Beta-amyloid protein 40 (1 entity in total)
• 機能のキーワード: 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: 4335.85

構造登録者

Vivekanandan, S.,Brender, J.R.,Lee, S.Y.,Ramamoorthy, A. (登録日: 2011-07-06, 公開日: 2011-07-20, 最終更新日: 2024-05-15)

主引用文献

Vivekanandan, S.,Brender, J.R.,Lee, S.Y.,Ramamoorthy, A.
A partially folded structure of amyloid-beta(1-40) in an aqueous environment.
Biochem.Biophys.Res.Commun., 411:312-316, 2011

PubMed Abstract: Aggregation of the Aβ(1-40) peptide is linked to the development of extracellular plaques characteristic of Alzheimer's disease. While previous studies commonly show the Aβ(1-40) is largely unstructured in solution, we show that Aβ(1-40) can adopt a compact, partially folded structure. In this structure (PDB ID: 2LFM), the central hydrophobic region of the peptide forms a 3(10) helix from H13 to D23 and the N- and C-termini collapse against the helix due to the clustering of hydrophobic residues. Helical intermediates have been predicted to be crucial on-pathway intermediates in amyloid fibrillogenesis, and the structure presented here presents a new target for investigation of early events in Aβ(1-40) fibrillogenesis.

PubMed: 21726530
DOI: 10.1016/j.bbrc.2011.06.133

実験手法

SOLUTION NMR