› 4yxl

X-ray diffraction
2.6Å resolution

Crystal structure of Syrian hamster prion protein complexed with POM1 FAB

Released:
DOI: 10.2210/pdb4yxl/pdb
PDB entry 4yxl coloured by chain, front view.
PDB entry 4yxl coloured by chain, side view.
PDB entry 4yxl coloured by chain, top view.
Source organisms:
Primary publication:
X-ray structural and molecular dynamical studies of the globular domains of cow, deer, elk and Syrian hamster prion proteins.
Baral PK, Swayampakula M, Aguzzi A, James MN
J Struct Biol 192 37-47 (2015)
PMID: 26320075

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-230433 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.9 KDa
Source organism: Mesocricetus auratus
Expression system: Escherichia coli
UniProt:
  • Canonical: P04273 (Residues: 90-232; Coverage: 62%)
Gene names: PRNP, PRP
Sequence domains: Prion/Doppel alpha-helical domain
POM1 FAB HEAVY CHAIN Chain: H
Molecule details ›
Chain: H
Length: 218 amino acids
Theoretical weight: 23.37 KDa
Source organism: Mus musculus
Expression system: Mus musculus
Structure domains: Immunoglobulins
POM1 FAB LIGHT CHAIN Chain: L
Molecule details ›
Chain: L
Length: 213 amino acids
Theoretical weight: 23.51 KDa
Source organism: Mus musculus
Expression system: Mus musculus
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: C2
Unit cell:
a: 83.916Å b: 105.969Å c: 76.326Å
α: 90° β: 95.37° γ: 90°
R-values:
R R work R free
0.264 0.262 0.31
Expression systems:
  • Escherichia coli
  • Mus musculus

Quick links

Citations

2 review citations

Conformational selection in amyloid-based immunotherapy: Survey of crystal structures of antibody-amyloid complexes.
Ma et al. (2016)
1 more

2 mentions without citation

The Neural Gut-Brain Axis of Pathological Protein Aggregation in Parkinson's Disease and Its Counterpart in Peroral Prion Infections.
Beekes M. (2021)
1 more