› 1xyk

Solution NMR

NMR Structure of the canine prion protein

Released:
DOI: 10.2210/pdb1xyk/pdb
PDB entry 1xyk coloured by chain, ensemble of 20 models, front view.
PDB entry 1xyk coloured by chain, ensemble of 20 models, side view.
PDB entry 1xyk coloured by chain, ensemble of 20 models, top view.
Source organism: Canis lupus familiaris
Primary publication:
Prion protein NMR structures of cats, dogs, pigs, and sheep.
Lysek DA, Schorn C, Nivon LG, Esteve-Moya V, Christen B, Calzolai L, von Schroetter C, Fiorito F, Herrmann T, Güntert P, Wüthrich K
Proc Natl Acad Sci U S A 102 640-5 (2005)
PMID: 15647367

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-129222 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 111 amino acids
Theoretical weight: 13.08 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O46501 (Residues: 124-195, 196-233; Coverage: 48%)
Gene names: 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

Quick links

Citations

28 review citations

Physiology of the prion protein.
Linden et al. (2008)
27 more

16 mentions without citation

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