4E1H

Fragment of human prion protein

4E1H の概要

• エントリーDOI: 10.2210/pdb4e1h/pdb
• 関連するPDBエントリー: 4E1I
• 分子名称: Major prion protein, FE (III) ION, CITRIC ACID, ... (5 entities in total)
• 機能のキーワード: beta prism, amyloid-related oligomer, protein fibril, cell cycle
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell membrane; Lipid-anchor, GPI-anchor . Isoform 2: Cytoplasm : P04156 P04156
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 9483.88

構造登録者

Apostol, M.I.,Perry, K.,Surewicz, W.K. (登録日: 2012-03-06, 公開日: 2013-03-06, 最終更新日: 2024-10-16)

主引用文献

Apostol, M.I.,Perry, K.,Surewicz, W.K.
Crystal structure of a human prion protein fragment reveals a motif for oligomer formation.
J.Am.Chem.Soc., 135:10202-10205, 2013

PubMed Abstract: The structural transition of the prion protein from α-helical- to β-sheet-rich underlies its conversion into infectious and disease-associated isoforms. Here we describe the crystal structure of a fragment from human prion protein consisting of the disulfide-bond-linked portions of helices 2 and 3. Instead of forming a pair-of-sheets steric zipper structure characteristic of amyloid fibers, this fragment crystallized into a β-sheet-rich assembly of hexameric oligomers. This study reveals a never before observed structural motif for ordered protein aggregates and suggests a possible mechanism for self-propagation of misfolded conformations by such nonamyloid oligomers.

PubMed: 23808589
DOI: 10.1021/ja403001q

実験手法

X-RAY DIFFRACTION (1.4 Å)