2LBG

Structure of the CHR of the Prion protein in DPC Micelles

2LBG の概要

• エントリーDOI: 10.2210/pdb2lbg/pdb
• NMR情報: BMRB: 17558
• 分子名称: Major prion protein (1 entity in total)
• 機能のキーワード: prion protein, conserved hydrophobic region, membrane protein
• 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: 1
• 化学式量合計: 2494.94

構造登録者

Sauve, S.,Aubin, Y. (登録日: 2011-03-31, 公開日: 2011-12-07, 最終更新日: 2024-05-15)

主引用文献

Sauve, S.,Buijs, D.,Gingras, G.,Aubin, Y.
Interactions between the Conserved Hydrophobic Region of the Prion Protein and Dodecylphosphocholine Micelles.
J.Biol.Chem., 287:1915-1922, 2012

PubMed Abstract: The three-dimensional structure of PrP110-136, a peptide encompassing the conserved hydrophobic region of the human prion protein, has been determined at high resolution in dodecylphosphocholine micelles by NMR. The results support the conclusion that the (Ctm)PrP, a transmembrane form of the prion protein, adopts a different conformation than the reported structures of the normal prion protein determined in solution. Paramagnetic relaxation enhancement studies with gadolinium-diethylenetriaminepentaacetic acid indicated that the conserved hydrophobic region peptide is not inserted symmetrically in the micelle, thus suggesting the presence of a guanidium-phosphate ion pair involving the side chain of the terminal arginine and the detergent headgroup. Titration of dodecylphosphocholine into a solution of PrP110-136 revealed the presence of a surface-bound species. In addition, paramagnetic probes located the surface-bound peptide somewhere below the micelle-water interface when using the inserted helix as a positional reference. This localization of the unknown population would allow a similar ion pair interaction.

PubMed: 22128151
DOI: 10.1074/jbc.M111.279364

実験手法

SOLUTION NMR