› 2k56

Solution NMR

Bank Vole Prion Protein (121-231)

Released:
DOI: 10.2210/pdb2k56/pdb
PDB entry 2k56 coloured by chain, ensemble of 20 models, front view.
PDB entry 2k56 coloured by chain, ensemble of 20 models, side view.
PDB entry 2k56 coloured by chain, ensemble of 20 models, top view.
Source organism: Myodes glareolus
Primary publication:
NMR structure of the bank vole prion protein at 20 degrees C contains a structured loop of residues 165-171.
Christen B, Pérez DR, Hornemann S, Wüthrich K
J Mol Biol 383 306-12 (2008)
PMID: 18773909

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186590 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 113 amino acids
Theoretical weight: 13.24 KDa
Source organism: Myodes glareolus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8VHV5 (Residues: 121-231; Coverage: 49%)
Gene name: PrP
Sequence domains: Prion/Doppel alpha-helical domain
Structure domains: Prion/Doppel protein, beta-ribbon domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: OPAL (water shell), TORSION ANGLE DYNAMICS,
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Prion protein misfolding and disease.
Moore et al. (2009)
4 more

6 mentions without citation

Discordant and chameleon sequences: their distribution and implications for amyloidogenicity.
Gendoo et al. (2011)
5 more