› 1h0l

Solution NMR

HUMAN PRION PROTEIN 121-230 M166C/E221C

Released:
DOI: 10.2210/pdb1h0l/pdb
PDB entry 1h0l coloured by chain, ensemble of 20 models, front view.
PDB entry 1h0l coloured by chain, ensemble of 20 models, side view.
PDB entry 1h0l coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
NMR structure of a variant human prion protein with two disulfide bridges.
Zahn R, G��ntert P, von Schroetter C, W��thrich K
J. Mol. Biol. 326 225-34 (2003)
PMID: 12547204

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: 112 amino acids
Theoretical weight: 13.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04156 (Residues: 119-230; Coverage: 49%)
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: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Implications of peptide assemblies in amyloid diseases.
Ke et al. (2017)
2 more

1 mention without citation

The landscape of the prion protein's structural response to mutation revealed by principal component analysis of multiple NMR ensembles.
Gendoo et al. (2012)