7O1Q

Amyloid beta oligomer displayed on the alpha hemolysin scaffold

7O1Q の概要

• エントリーDOI: 10.2210/pdb7o1q/pdb
• EMDBエントリー: 12696
• 分子名称: Alpha-hemolysin hybridized Abeta (1 entity in total)
• 機能のキーワード: amyloid beta oligomer, alpha hemolysin, alzheimer's disease, toxin
• 由来する生物種: Staphylococcus aureus; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 234214.89

構造登録者

Wu, J.,Blum, T.B.,Farrell, D.P.,DiMaio, F.,Abrahams, J.P.,Luo, J. (登録日: 2021-03-30, 公開日: 2021-04-14, 最終更新日: 2024-07-10)

主引用文献

Wu, J.,Blum, T.B.,Farrell, D.P.,DiMaio, F.,Abrahams, J.P.,Luo, J.
Cryo-electron Microscopy Imaging of Alzheimer's Amyloid-beta 42 Oligomer Displayed on a Functionally and Structurally Relevant Scaffold.
Angew.Chem.Int.Ed.Engl., 60:18680-18687, 2021

PubMed Abstract: Amyloid-β peptide (Aβ) oligomers are pathogenic species of amyloid aggregates in Alzheimer's disease. Like certain protein toxins, Aβ oligomers permeabilize cellular membranes, presumably through a pore formation mechanism. Owing to their structural and stoichiometric heterogeneity, the structure of these pores remains to be characterized. We studied a functional Aβ42-pore equivalent, created by fusing Aβ42 to the oligomerizing, soluble domain of the α-hemolysin (αHL) toxin. Our data reveal Aβ42-αHL oligomers to share major structural, functional, and biological properties with wild-type Aβ42-pores. Single-particle cryo-EM analysis of Aβ42-αHL oligomers (with an overall 3.3 Å resolution) reveals the Aβ42-pore region to be intrinsically flexible. The Aβ42-αHL oligomers will allow many of the features of the wild-type amyloid oligomers to be studied that cannot be otherwise, and may be a highly specific antigen for the development of immuno-base diagnostics and therapies.

PubMed: 34042235
DOI: 10.1002/anie.202104497

実験手法

ELECTRON MICROSCOPY (3.4 Å)