6WXM

X-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 16-36

6WXM の概要

• エントリーDOI: 10.2210/pdb6wxm/pdb
• 分子名称: Amyloid-beta protein, HEXANE-1,6-DIOL (3 entities in total)
• 機能のキーワード: oligomer, alzheimer's, de novo protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 28536.03

構造登録者

Kreutzer, A.G.,Nowick, J.S. (登録日: 2020-05-11, 公開日: 2020-07-08, 最終更新日: 2025-04-02)

主引用文献

Kreutzer, A.G.,Samdin, T.D.,Guaglianone, G.,Spencer, R.K.,Nowick, J.S.
X-ray Crystallography Reveals Parallel and Antiparallel beta-Sheet Dimers of a beta-Hairpin Derived from A beta16-36that Assemble to Form Different Tetramers.
Acs Chem Neurosci, 11:2340-2347, 2020

PubMed Abstract: High-resolution structures of oligomers formed by the β-amyloid peptide, Aβ, are important for understanding the molecular basis of Alzheimer's disease. Dimers of Aβ are linked to the pathogenesis and progression of Alzheimer's disease, and tetramers of Aβ are neurotoxic. This paper reports the X-ray crystallographic structures of dimers and tetramers, as well as an octamer, formed by a peptide derived from the central and -terminal regions of Aβ. In the crystal lattice, the peptide assembles to form two different dimers-an antiparallel β-sheet dimer and a parallel β-sheet dimer-that each further self-assemble to form two different tetramers-a sandwich-like tetramer and a twisted β-sheet tetramer. The structures of these dimers and tetramers derived from Aβ serve as potential models for dimers and tetramers of full-length Aβ that form and in Alzheimer's disease-afflicted brains.

PubMed: 32584538
DOI: 10.1021/acschemneuro.0c00290

実験手法

X-RAY DIFFRACTION (2.3 Å)