3NVG

MIHFGN segment 137-142 from mouse prion

3NVG の概要

• エントリーDOI: 10.2210/pdb3nvg/pdb
• 関連するPDBエントリー: 3NVE 3NVF 3NVH
• 分子名称: Major prion protein (2 entities in total)
• 機能のキーワード: amyloid-like protofibril, protein fibril
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cell membrane; Lipid-anchor, GPI-anchor: P04925
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 718.84

構造登録者

Apostol, M.I.,Sawaya, M.R.,Eisenberg, D. (登録日: 2010-07-08, 公開日: 2011-03-02, 最終更新日: 2024-02-21)

主引用文献

Apostol, M.I.,Wiltzius, J.J.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.
Atomic structures suggest determinants of transmission barriers in Mammalian prion disease.
Biochemistry, 50:2456-2463, 2011

PubMed Abstract: Prion represents a unique class of pathogens devoid of nucleic acid. The deadly diseases transmitted by it between members of one species and, in certain instances, to members of other species present a public health concern. Transmissibility and the barriers to transmission between species have been suggested to arise from the degree to which a pathological protein conformation from an individual of one species can seed a pathological conformation in another species. However, this hypothesis has never been illustrated at an atomic level. Here we present three X-ray atomic structures of the same segment from human, mouse, and hamster PrP, which is critical for forming amyloid and confers species specificity in PrP seeding experiments. The structures reveal that different sequences encode different steric zippers and suggest that the degree of dissimilarity of these zipper structures gives rise to transmission barriers in prion disease, such as those that protect humans from acquiring bovine spongiform encephalopathy (BSE) and chronic wasting disease (CWD).

PubMed: 21323366
DOI: 10.1021/bi101803k

実験手法

X-RAY DIFFRACTION (1.48 Å)