› 1fo7

Solution NMR

HUMAN PRION PROTEIN MUTANT E200K FRAGMENT 90-231

Released:
DOI: 10.2210/pdb1fo7/pdb
PDB entry 1fo7 coloured by chain, ensemble of 30 models, front view.
PDB entry 1fo7 coloured by chain, ensemble of 30 models, side view.
PDB entry 1fo7 coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases.
Zhang Y, Swietnicki W, Zagorski MG, Surewicz WK, Sönnichsen FD
J Biol Chem 275 33650-4 (2000)
PMID: 10954699

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-137455 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 142 amino acids
Theoretical weight: 16.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04156 (Residues: 90-231; Coverage: 62%)
Gene names: ALTPRP, PRIP, 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

19 review citations

Peptide aggregation in neurodegenerative disease.
Murphy RM. (2002)
18 more

9 mentions without citation

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