7YPG

Cryo-EM structure of amyloid fibril formed by tau (297-391)

7YPG の概要

• エントリーDOI: 10.2210/pdb7ypg/pdb
• EMDBエントリー: 33999
• 分子名称: Isoform Tau-E of Microtubule-associated protein tau (1 entity in total)
• 機能のキーワード: amyloid fibril, protein fibril
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 61912.86

構造登録者

Zhang, S.Q.,Li, X.,Liu, C. (登録日: 2022-08-03, 公開日: 2022-12-14, 最終更新日: 2024-05-01)

主引用文献

Li, X.,Zhang, S.,Liu, Z.,Tao, Y.,Xia, W.,Sun, Y.,Liu, C.,Le, W.,Sun, B.,Li, D.
Subtle change of fibrillation condition leads to substantial alteration of recombinant Tau fibril structure.
Iscience, 25:105645-105645, 2022

PubMed Abstract: assembly of amyloid fibrils that recapitulate those in human brains is very useful for fundamental and applied research on the amyloid formation, pathology, and clinical detection. Recent success in the assembly of Tau fibrils enables the recapitulation of the paired helical filament (PHF) of Tau extracted from brains of patients with Alzheimer's disease (AD). However, following the protocol, we observed that Tau constructs including 297-391 and a mixture of 266-391 (3R)/297-391, which are expected to predominantly form PHF-like fibrils, form highly heterogeneous fibrils instead. Moreover, the seemingly PHF-like fibril formed by Tau 297-391 exhibits a distinctive atomic structure with a spindle-like fold, that is neither PHF-like or similar to any known Tau fibril structures revealed by cryo-electron microscopy (cryo-EM). Our work highlights the high sensitivity of amyloid fibril formation to subtle conditional changes and suggests high-resolution structural characterization to assembled fibrils prior to further laboratory use.

PubMed: 36505939
DOI: 10.1016/j.isci.2022.105645

実験手法

ELECTRON MICROSCOPY (2.5 Å)