2LBG

Structure of the CHR of the Prion protein in DPC Micelles

Summary for 2LBG

• Entry DOI: 10.2210/pdb2lbg/pdb
• NMR Information: BMRB: 17558
• Descriptor: Major prion protein (1 entity in total)
• Functional Keywords: prion protein, conserved hydrophobic region, membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor. Isoform 2: Cytoplasm: P04156
• Total number of polymer chains: 1
• Total formula weight: 2494.94

Authors

Sauve, S.,Aubin, Y. (deposition date: 2011-03-31, release date: 2011-12-07, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR