2KU4

Horse prion protein

2KU4 の概要

• エントリーDOI: 10.2210/pdb2ku4/pdb
• 関連するPDBエントリー: 2KU5 2KU6
• NMR情報: BMRB: 16720
• 分子名称: Major prion protein (1 entity in total)
• 機能のキーワード: ecprp, prion, horse, equus caballus, amyloid, cell membrane, membrane, membrane protein
• 由来する生物種: Equus caballus (horse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13203.70

構造登録者

Perez, D.R.,Damberger, F.F.,Wuthrich, K. (登録日: 2010-02-12, 公開日: 2010-06-09, 最終更新日: 2024-10-16)

主引用文献

Perez, D.R.,Damberger, F.F.,Wuthrich, K.
Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein.
J.Mol.Biol., 400:121-128, 2010

PubMed Abstract: The NMR structure of the horse (Equus caballus) cellular prion protein at 25 degrees C exhibits the typical PrP(C) [cellular form of prion protein (PrP)] global architecture, but in contrast to most other mammalian PrP(C)s, it contains a well-structured loop connecting the beta2 strand with the alpha2 helix. Comparison with designed variants of the mouse prion protein resulted in the identification of a single amino acid exchange within the loop, D167S, which correlates with the high structural order of this loop in the solution structure at 25 degrees C and is unique to the PrP sequences of equine species. The beta2-alpha2 loop and the alpha3 helix form a protein surface epitope that has been proposed to be the recognition area for a hypothetical chaperone, "protein X," which would promote conversion of PrP(C) into the disease-related scrapie form and thus mediate intermolecular interactions related to the transmission barrier for transmissible spongiform encephalopathies (TSEs) between different species. The present results are evaluated in light of recent indications from in vivo experiments that the local beta2-alpha2 loop structure affects the susceptibility of transgenic mice to TSEs and the fact that there are no reports on TSE in horses.

PubMed: 20460128
DOI: 10.1016/j.jmb.2010.04.066

実験手法

SOLUTION NMR