› 1hjm

Solution NMR

HUMAN PRION PROTEIN AT PH 7.0

Released:
DOI: 10.2210/pdb1hjm/pdb
PDB entry 1hjm coloured by chain, front view.
PDB entry 1hjm coloured by chain, side view.
PDB entry 1hjm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Influence of pH on NMR structure and stability of the human prion protein globular domain.
Calzolai L, Zahn R
J Biol Chem 278 35592-6 (2003)
PMID: 12826672

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: 104 amino acids
Theoretical weight: 12.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04156 (Residues: 125-228; Coverage: 45%)
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
Chemical shift assignment: 79%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Genetic Creutzfeldt-Jakob disease and fatal familial insomnia: insights into phenotypic variability and disease pathogenesis.
Capellari et al. (2011)
8 more

14 mentions without citation

The consequences of pathogenic mutations to the human prion protein.
van der Kamp et al. (2009)
13 more