› 2ku5

Solution NMR

Mouse Prion Protein (121-231) with mutation D167S

Released:
DOI: 10.2210/pdb2ku5/pdb
PDB entry 2ku5 coloured by chain, ensemble of 20 models, front view.
PDB entry 2ku5 coloured by chain, ensemble of 20 models, side view.
PDB entry 2ku5 coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein.
Pérez DR, Damberger FF, Wüthrich K
J Mol Biol 400 121-8 (2010)
PMID: 20460128

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-138267 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 113 amino acids
Theoretical weight: 13.32 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P04925 (Residues: 120-231; Coverage: 48%)
Gene names: Prn-p, Prnp, 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
Chemical shift assignment: 84%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Allosteric function and dysfunction of the prion protein.
Linden et al. (2012)
15 more

3 mentions without citation

Cellular prion protein conformation and function.
Damberger et al. (2011)
2 more