5OQV

Near-atomic resolution fibril structure of complete amyloid-beta(1-42) by cryo-EM

5OQV の概要

• エントリーDOI: 10.2210/pdb5oqv/pdb
• EMDBエントリー: 3851
• NMR情報: BMRB: 27212
• 分子名称: Amyloid beta A4 protein (1 entity in total)
• 機能のキーワード: amyloid, fibril, aggregation, alzheimer's disease, 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: 9
• 化学式量合計: 40680.78

構造登録者

Gremer, L.,Schoelzel, D.,Schenk, C.,Reinartz, E.,Labahn, J.,Ravelli, R.,Tusche, M.,Lopez-Iglesias, C.,Hoyer, W.,Heise, H.,Willbold, D.,Schroeder, G.F. (登録日: 2017-08-14, 公開日: 2017-09-13, 最終更新日: 2024-05-15)

主引用文献

Gremer, L.,Scholzel, D.,Schenk, C.,Reinartz, E.,Labahn, J.,Ravelli, R.B.G.,Tusche, M.,Lopez-Iglesias, C.,Hoyer, W.,Heise, H.,Willbold, D.,Schroder, G.F.
Fibril structure of amyloid-beta (1-42) by cryo-electron microscopy.
Science, 358:116-119, 2017

PubMed Abstract: Amyloids are implicated in neurodegenerative diseases. Fibrillar aggregates of the amyloid-β protein (Aβ) are the main component of the senile plaques found in brains of Alzheimer's disease patients. We present the structure of an Aβ(1-42) fibril composed of two intertwined protofilaments determined by cryo-electron microscopy (cryo-EM) to 4.0-angstrom resolution, complemented by solid-state nuclear magnetic resonance experiments. The backbone of all 42 residues and nearly all side chains are well resolved in the EM density map, including the entire N terminus, which is part of the cross-β structure resulting in an overall "LS"-shaped topology of individual subunits. The dimer interface protects the hydrophobic C termini from the solvent. The characteristic staggering of the nonplanar subunits results in markedly different fibril ends, termed "groove" and "ridge," leading to different binding pathways on both fibril ends, which has implications for fibril growth.

PubMed: 28882996
DOI: 10.1126/science.aao2825

実験手法

ELECTRON MICROSCOPY (4 Å)