2LBG: Structure of the CHR of the Prion Protein in DPC Micelles

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.
PDB ID: 2LBGDownload
MMDB ID: 95477
PDB Deposition Date: 2011/3/31
Updated in MMDB: 2011/12 
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2LBG: monomeric; determined by author
Molecular Components in 2LBG
Label Count Molecule
Protein (1 molecule)
Major Prion Protein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB