› 4yxh

X-ray diffraction
2.7Å resolution

Crystal structure of Deer prion protein complexed with POM1 FAB

Released:
DOI: 10.2210/pdb4yxh/pdb
PDB entry 4yxh coloured by chain, front view.
PDB entry 4yxh coloured by chain, side view.
PDB entry 4yxh 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-230431 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 135 amino acids
Theoretical weight: 15.96 KDa
Source organism: Odocoileus hemionus
Expression system: Escherichia coli
UniProt:
  • Canonical: P47852 (Residues: 124-231; Coverage: 47%)
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: 23.4 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 BL9-2
Spacegroup: C2
Unit cell:
a: 84.282Å b: 106.58Å c: 75.775Å
α: 90° β: 95.81° γ: 90°
R-values:
R R work R free
0.245 0.242 0.288
Expression systems:
  • Escherichia coli
  • Mus musculus

Quick links

Citations

3 review citations

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

4 mentions without citation

Destabilizing polymorphism in cervid prion protein hydrophobic core determines prion conformation and conversion efficiency.
Hannaoui et al. (2017)
3 more