8OQ5

AApoAII amyloid fibril Morphology I (ex vivo)

8OQ5 の概要

• エントリーDOI: 10.2210/pdb8oq5/pdb
• EMDBエントリー: 17105
• 分子名称: Apolipoprotein A-II (1 entity in total)
• 機能のキーワード: amyloid, protein fibril, systemic amyloidosis, misfolding disease, helical
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 104960.74

構造登録者

Andreotti, G.,Schmidt, M.,Faendrich, M. (登録日: 2023-04-11, 公開日: 2024-02-21)

主引用文献

Andreotti, G.,Baur, J.,Ugrina, M.,Pfeiffer, P.B.,Hartmann, M.,Wiese, S.,Miyahara, H.,Higuchi, K.,Schwierz, N.,Schmidt, M.,Fandrich, M.
Insights into the Structural Basis of Amyloid Resistance Provided by Cryo-EM Structures of AApoAII Amyloid Fibrils.
J.Mol.Biol., 436:168441-168441, 2024

PubMed Abstract: Amyloid resistance is the inability or the reduced susceptibility of an organism to develop amyloidosis. In this study we have analysed the molecular basis of the resistance to systemic AApoAII amyloidosis, which arises from the formation of amyloid fibrils from apolipoprotein A-II (ApoA-II). The disease affects humans and animals, including SAMR1C mice that express the C allele of ApoA-II protein, whereas other mouse strains are resistant to development of amyloidosis due to the expression of other ApoA-II alleles, such as ApoA-IIF. Using cryo-electron microscopy, molecular dynamics simulations and other methods, we have determined the structures of pathogenic AApoAII amyloid fibrils from SAMR1C mice and analysed the structural effects of ApoA-IIF-specific mutational changes. Our data show that these changes render ApoA-IIF incompatible with the specific fibril morphologies, with which ApoA-II protein can become pathogenic in vivo.

PubMed: 38199491
DOI: 10.1016/j.jmb.2024.168441

実験手法

ELECTRON MICROSCOPY (2.4 Å)