1XYU

Solution structure of the sheep prion protein with polymorphism H168

1XYU の概要

• エントリーDOI: 10.2210/pdb1xyu/pdb
• NMR情報: BMRB: 6381
• 分子名称: Major prion protein (1 entity in total)
• 機能のキーワード: prion, tse, ovprp, prp, unknown function
• 由来する生物種: Ovis aries (sheep)
• 細胞内の位置: Cell membrane; Lipid-anchor, GPI-anchor: P23907
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13097.54

構造登録者

Calzolai, L.,Lysek, D.A.,Guntert, P.,Wuthrich, K. (登録日: 2004-11-11, 公開日: 2005-01-04, 最終更新日: 2024-10-30)

主引用文献

Lysek, D.A.,Schorn, C.,Nivon, L.G.,Esteve-Moya, V.,Christen, B.,Calzolai, L.,von Schroetter, C.,Fiorito, F.,Herrmann, T.,Guntert, P.,Wuthrich, K.
Prion protein NMR structures of cats, dogs, pigs, and sheep
Proc.Natl.Acad.Sci.USA, 102:640-645, 2005

PubMed Abstract: The NMR structures of the recombinant cellular form of the prion proteins (PrPC) of the cat (Felis catus), dog (Canis familiaris), and pig (Sus scrofa), and of two polymorphic forms of the prion protein from sheep (Ovis aries) are presented. In all of these species, PrPC consists of an N-terminal flexibly extended tail with approximately 100 amino acid residues and a C-terminal globular domain of approximately 100 residues with three alpha-helices and a short antiparallel beta-sheet. Although this global architecture coincides with the previously reported murine, Syrian hamster, bovine, and human PrPC structures, there are local differences between the globular domains of the different species. Because the five newly determined PrPC structures originate from species with widely different transmissible spongiform encephalopathy records, the present data indicate previously uncharacterized possible correlations between local features in PrPC three-dimensional structures and susceptibility of different mammalian species to transmissible spongiform encephalopathies.

PubMed: 15647367
DOI: 10.1073/pnas.0408937102

実験手法

SOLUTION NMR