› 1tpx

X-ray diffraction
2.56Å resolution

Ovine recombinant PrP(114-234), ARQ variant in complex with the Fab of the VRQ14 antibody

Released:
DOI: 10.2210/pdb1tpx/pdb
PDB entry 1tpx coloured by chain, front view.
PDB entry 1tpx coloured by chain, side view.
PDB entry 1tpx coloured by chain, top view.
Source organisms:
Primary publication:
Insight into the PrPC-->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants.
Eghiaian F, Grosclaude J, Lesceu S, Debey P, Doublet B, Tréguer E, Rezaei H, Knossow M
Proc Natl Acad Sci U S A 101 10254-9 (2004)
PMID: 15240887

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-210869 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 13.87 KDa
Source organism: Ovis aries
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P23907 (Residues: 114-234; Coverage: 52%)
Gene names: PRNP, PRP, SIP
Sequence domains: Prion/Doppel alpha-helical domain
Structure domains: Prion/Doppel protein, beta-ribbon domain
the VRQ14 Fab Chain: B
Molecule details ›
Chain: B
Length: 212 amino acids
Theoretical weight: 22.81 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
the VRQ14 Fab Chain: C
Molecule details ›
Chain: C
Length: 219 amino acids
Theoretical weight: 24.16 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P21212
Unit cell:
a: 91.77Å b: 145.593Å c: 43.029Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.282
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 review citations

Copper and the prion protein: methods, structures, function, and disease.
Millhauser GL. (2007)
13 more

14 mentions without citation

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