7JQU

Abeta 16-36 beta-hairpin mimic with E22G Arctic mutation

これはPDB形式変換不可エントリーです。

7JQU の概要

• エントリーDOI: 10.2210/pdb7jqu/pdb
• 分子名称: Abeta 16-36 beta-hairpin mimic VAL-ORN-LYS-LEU-VAL-MEA-PHE-ALA-GLN-ORN-ALA-ILE-ILE-GLY-LEU-MET (2 entities in total)
• 機能のキーワード: alzheimer's disease, amyloid, abeta, oligomer, familial mutant, de novo protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 5379.86

構造登録者

Kreutzer, A.G.,McKnelly, K.J.,Nowick, J.S. (登録日: 2020-08-11, 公開日: 2021-09-08, 最終更新日: 2023-10-18)

主引用文献

McKnelly, K.J.,Kreutzer, A.G.,Howitz, W.J.,Haduong, K.,Yoo, S.,Hart, C.,Nowick, J.S.
Effects of Familial Alzheimer's Disease Mutations on the Assembly of a beta-Hairpin Peptide Derived from A beta 16-36 .
Biochemistry, 61:446-454, 2022

PubMed Abstract: Familial Alzheimer's disease (FAD) is associated with mutations in the β-amyloid peptide (Aβ) or the amyloid precursor protein (APP). FAD mutations of Aβ were incorporated into a macrocyclic peptide that mimics a β-hairpin to study FAD point mutations K16N, A21G, E22Δ, E22G, E22Q, E22K, and L34V and their effect on assembly, membrane destabilization, and cytotoxicity. The X-ray crystallographic structures of the four E22 mutant peptides reveal that the peptides assemble to form the same compact hexamer. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) experiments reveal that the mutant FAD peptides assemble as trimers or hexamers, with peptides that have greater positive charge assembling as more stable hexamers. Mutations that increase the positive charge also increase the cytotoxicity of the peptides and their propensity to destabilize lipid membranes.

PubMed: 35213141
DOI: 10.1021/acs.biochem.1c00664

実験手法

X-RAY DIFFRACTION (2.611 Å)