› 2n53

Solution NMR

Solution structure of ovis aries prp

Released:
DOI: 10.2210/pdb2n53/pdb
PDB entry 2n53 coloured by chain, ensemble of 20 models, front view.
PDB entry 2n53 coloured by chain, ensemble of 20 models, side view.
PDB entry 2n53 coloured by chain, ensemble of 20 models, top view.
Source organism: Ovis aries
Primary publication:
Generating Bona Fide Mammalian Prions with Internal Deletions.
Munoz-Montesino C, Sizun C, Moudjou M, Herzog L, Reine F, Chapuis J, Ciric D, Igel-Egalon A, Laude H, Béringue V, Rezaei H, Dron M
J Virol 90 6963-6975 (2016)
PMID: 27226369

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: 154 amino acids
Theoretical weight: 17.54 KDa
Source organism: Ovis aries
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P23907 (Residues: 103-234; Coverage: 57%)
Gene names: PRNP, PRP, SIP
Sequence domains: Prion/Doppel alpha-helical domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 53%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Prion Strains and Transmission Barrier Phenomena.
Igel-Egalon et al. (2018)
1 more

2 mentions without citation

Generating Bona Fide Mammalian Prions with Internal Deletions.
Munoz-Montesino et al. (2016)
1 more