3NHD

GYVLGS segment 127-132 from human prion with V129

3NHD の概要

• エントリーDOI: 10.2210/pdb3nhd/pdb
• 関連するPDBエントリー: 3NHC
• 分子名称: Major prion protein, ACETIC ACID (3 entities in total)
• 機能のキーワード: amyloid-like protofibril, protein fibril
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Lipid-anchor, GPI-anchor. Isoform 2: Cytoplasm: P04156
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 1309.42

構造登録者

Apostol, M.I.,Eisenberg, D. (登録日: 2010-06-14, 公開日: 2010-08-04, 最終更新日: 2024-05-22)

主引用文献

Apostol, M.I.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.
Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease.
J.Biol.Chem., 285:29671-29675, 2010

PubMed Abstract: A single nucleotide polymorphism (SNP) in codon 129 of the human prion gene, leading to a change from methionine to valine at residue 129 of prion protein (PrP), has been shown to be a determinant in the susceptibility to prion disease. However, the molecular basis of this effect remains unexplained. In the current study, we determined crystal structures of prion segments having either Met or Val at residue 129. These 6-residue segments of PrP centered on residue 129 are "steric zippers," pairs of interacting β-sheets. Both structures of these "homozygous steric zippers" reveal direct intermolecular interactions between Met or Val in one sheet and the identical residue in the mating sheet. These two structures, plus a structure-based model of the heterozygous Met-Val steric zipper, suggest an explanation for the previously observed effects of this locus on prion disease susceptibility and progression.

PubMed: 20685658
DOI: 10.1074/jbc.C110.158303

実験手法

X-RAY DIFFRACTION (1.92 Å)