3PZZ

Structure of an amyloid forming peptide GAIIGL (29-34) from amyloid beta

3PZZ の概要

• エントリーDOI: 10.2210/pdb3pzz/pdb
• 分子名称: Amyloid beta A4 protein (2 entities in total)
• 機能のキーワード: amyloid protofibril, 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: 2
• 化学式量合計: 1085.34

構造登録者

Soriaga, A.B.,Laganowsky, A.L.,Sawaya, M.R.,Eisenberg, D. (登録日: 2010-12-14, 公開日: 2011-10-12, 最終更新日: 2024-02-21)

主引用文献

Colletier, J.P.,Laganowsky, A.,Landau, M.,Zhao, M.,Soriaga, A.B.,Goldschmidt, L.,Flot, D.,Cascio, D.,Sawaya, M.R.,Eisenberg, D.
Molecular basis for amyloid-beta polymorphism.
Proc.Natl.Acad.Sci.USA, 108:16938-16943, 2011

PubMed Abstract: Amyloid-beta (Aβ) aggregates are the main constituent of senile plaques, the histological hallmark of Alzheimer's disease. Aβ molecules form β-sheet containing structures that assemble into a variety of polymorphic oligomers, protofibers, and fibers that exhibit a range of lifetimes and cellular toxicities. This polymorphic nature of Aβ has frustrated its biophysical characterization, its structural determination, and our understanding of its pathological mechanism. To elucidate Aβ polymorphism in atomic detail, we determined eight new microcrystal structures of fiber-forming segments of Aβ. These structures, all of short, self-complementing pairs of β-sheets termed steric zippers, reveal a variety of modes of self-association of Aβ. Combining these atomic structures with previous NMR studies allows us to propose several fiber models, offering molecular models for some of the repertoire of polydisperse structures accessible to Aβ. These structures and molecular models contribute fundamental information for understanding Aβ polymorphic nature and pathogenesis.

PubMed: 21949245
DOI: 10.1073/pnas.1112600108

実験手法

X-RAY DIFFRACTION (1.29 Å)