1Y16

mouse prion protein with mutations S170N and N174T

1Y16 の概要

• エントリーDOI: 10.2210/pdb1y16/pdb
• 関連するPDBエントリー: 1XYW 1XYX 1Y15
• 分子名称: Major prion protein (1 entity in total)
• 機能のキーワード: prion protein, prp, prnp, tse, cwd, unknown function
• 由来する生物種: Mus musculus (house 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: 13278.77

構造登録者

Gossert, A.D.,Bonjour, S.,Lysek, D.A.,Fiorito, F.,Wuthrich, K. (登録日: 2004-11-17, 公開日: 2005-01-25, 最終更新日: 2024-10-23)

主引用文献

Gossert, A.D.,Bonjour, S.,Lysek, D.A.,Fiorito, F.,Wuthrich, K.
Prion protein NMR structures of elk and of mouse/elk hybrids
Proc.Natl.Acad.Sci.Usa, 102:646-650, 2005

PubMed Abstract: The NMR structure of the recombinant elk prion protein (ePrP), which represents the cellular isoform (ePrPC) in the healthy organism, is described here. As anticipated from the highly conserved amino acid sequence, ePrPC has the same global fold as other mammalian prion proteins (PrPs), with a flexibly disordered "tail" of residues 23-124 and a globular domain 125-226 with three alpha-helices and a short antiparallel beta-sheet. However, ePrPC shows a striking local structure variation when compared with most other mammalian PrPs, in particular human, bovine, and mouse PrPC. A loop of residues 166-175, which links the beta-sheet with the alpha2-helix and is part of a hypothetical "protein X" epitope, is outstandingly well defined, whereas this loop is disordered in the other species. Based on NMR structure determinations of two mouse PrP variants, mPrP[N174T] and mPrP[S170N,N174T], this study shows that the structured loop in ePrPC relates to these two local amino acid exchanges, so that mPrP[S170N,N174T] exactly mimics ePrPC. These results are evaluated in the context of recent reports on chronic wasting disease (CWD) in captive and free-ranging deer and elk in the U.S. and Canada, and an animal model is proposed for support of future research on CWD.

PubMed: 15647363
DOI: 10.1073/pnas.0409008102

実験手法

SOLUTION NMR