› 1dx1

Solution NMR

BOVINE PRION PROTEIN RESIDUES 23-230

Released:
DOI: 10.2210/pdb1dx1/pdb
PDB entry 1dx1 coloured by chain, ensemble of 20 models, front view.
PDB entry 1dx1 coloured by chain, ensemble of 20 models, side view.
PDB entry 1dx1 coloured by chain, ensemble of 20 models, top view.
Source organism: Bos taurus
Primary publication:
NMR structure of the bovine prion protein.
López Garcia F, Zahn R, Riek R, Wüthrich K
Proc Natl Acad Sci U S A 97 8334-9 (2000)
PMID: 10899999

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145256 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 23.65 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P10279 (Residues: 25-241; Coverage: 90%)
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(DE3)

Quick links

Citations

33 review citations

Solid-state NMR studies of amyloid fibril structure.
Tycko R. (2011)
32 more

9 mentions without citation

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