6UUR

Human prion protein fibril, M129 variant

6UUR の概要

• エントリーDOI: 10.2210/pdb6uur/pdb
• EMDBエントリー: 20900
• 分子名称: Major prion protein (1 entity in total)
• 機能のキーワード: amyloid, fibril, prion, filament, protein fibril, fiber, prp
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 96857.71

構造登録者

Glynn, C.,Sawaya, M.R.,Ge, P.,Zhou, Z.H.,Rodriguez, J.A. (登録日: 2019-10-31, 公開日: 2020-04-15, 最終更新日: 2025-05-21)

主引用文献

Glynn, C.,Sawaya, M.R.,Ge, P.,Gallagher-Jones, M.,Short, C.W.,Bowman, R.,Apostol, M.,Zhou, Z.H.,Eisenberg, D.S.,Rodriguez, J.A.
Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core.
Nat.Struct.Mol.Biol., 27:417-423, 2020

PubMed Abstract: Self-templating assemblies of the human prion protein are clinically associated with transmissible spongiform encephalopathies. Here we present the cryo-EM structure of a denaturant- and protease-resistant fibril formed in vitro spontaneously by a 9.7-kDa unglycosylated fragment of the human prion protein. This human prion fibril contains two protofilaments intertwined with screw symmetry and linked by a tightly packed hydrophobic interface. Each protofilament consists of an extended beta arch formed by residues 106 to 145 of the prion protein, a hydrophobic and highly fibrillogenic disease-associated segment. Such structures of prion polymorphs serve as blueprints on which to evaluate the potential impact of sequence variants on prion disease.

PubMed: 32284600
DOI: 10.1038/s41594-020-0403-y

実験手法

ELECTRON MICROSCOPY (3.5 Å)