› 2ktm

Solution NMR

Solution NMR structure of H2H3 domain of ovine prion protein (residues 167-234)

Released:
DOI: 10.2210/pdb2ktm/pdb
PDB entry 2ktm coloured by chain, ensemble of 12 models, front view.
PDB entry 2ktm coloured by chain, ensemble of 12 models, side view.
PDB entry 2ktm coloured by chain, ensemble of 12 models, top view.
Source organism: Ovis aries
Primary publication:
Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3.
Adrover M, Pauwels K, Prigent S, de Chiara C, Xu Z, Chapuis C, Pastore A, Rezaei H
J Biol Chem 285 21004-12 (2010)
PMID: 20375014

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-150109 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 89 amino acids
Theoretical weight: 10.24 KDa
Source organism: Ovis aries
Expression system: Escherichia coli
UniProt:
  • Canonical: P23907 (Residues: 167-234; Coverage: 29%)
Gene names: PRNP, PRP, SIP
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: molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Prions and the potential transmissibility of protein misfolding diseases.
Kraus et al. (2013)
9 more

2 mentions without citation

Biochemical insight into the prion protein family.
Ciric et al. (2015)
1 more