› 1ag2

Solution NMR

PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, 2 MINIMIZED AVERAGE STRUCTURE

Released:
DOI: 10.2210/pdb1ag2/pdb
PDB entry 1ag2 coloured by chain, front view.
PDB entry 1ag2 coloured by chain, side view.
PDB entry 1ag2 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
NMR structure of the mouse prion protein domain PrP(121-231).
Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wüthrich K
Nature 382 180-2 (1996)
PMID: 8700211

Function and Biology Details

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

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: 103 amino acids
Theoretical weight: 12.35 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P04925 (Residues: 123-225; Coverage: 44%)
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
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

191 review citations

Prions.
Prusiner SB. (1998)
190 more

56 mentions without citation

A structural overview of the vertebrate prion proteins.
Pastore et al. (2007)
55 more