2L1D

Mouse prion protein (121-231) containing the substitution Y169G

2L1D の概要

• エントリーDOI: 10.2210/pdb2l1d/pdb
• 関連するPDBエントリー: 2L1E 2L1H 2L1K
• NMR情報: BMRB: 17081
• 分子名称: Major prion protein (1 entity in total)
• 機能のキーワード: prion, mutation, membrane protein
• 由来する生物種: Mus musculus (mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13302.75

構造登録者

Christen, B.,Damberger, F.F.,Perez, D.R.,Hornemann, S.,Wuthrich, K. (登録日: 2010-07-28, 公開日: 2011-08-10, 最終更新日: 2024-11-20)

主引用文献

Damberger, F.F.,Christen, B.,Perez, D.R.,Hornemann, S.,Wuthrich, K.
Cellular prion protein conformation and function.
Proc.Natl.Acad.Sci.USA, 108:17308-17313, 2011

PubMed Abstract: In the otherwise highly conserved NMR structures of cellular prion proteins (PrP(C)) from different mammals, species variations in a surface epitope that includes a loop linking a β-strand, β2, with a helix, α2, are associated with NMR manifestations of a dynamic equilibrium between locally different conformations. Here, it is shown that this local dynamic conformational polymorphism in mouse PrP(C) is eliminated through exchange of Tyr169 by Ala or Gly, but is preserved after exchange of Tyr 169 with Phe. NMR structure determinations of designed variants of mouse PrP(121-231) at 20 °C and of wild-type mPrP(121-231) at 37 °C together with analysis of exchange effects on NMR signals then resulted in the identification of the two limiting structures involved in this local conformational exchange in wild-type mouse PrP(C), and showed that the two exchanging structures present characteristically different solvent-exposed epitopes near the β2-α2 loop. The structural data presented in this paper provided a platform for currently ongoing, rationally designed experiments with transgenic laboratory animals for renewed attempts to unravel the so far elusive physiological function of the cellular prion protein.

PubMed: 21987789
DOI: 10.1073/pnas.1106325108

実験手法

SOLUTION NMR