› 4h88

X-ray diffraction
1.9Å resolution

Structure of POM1 FAB fragment complexed with mouse PrPc Fragment 120-230

Released:
DOI: 10.2210/pdb4h88/pdb
PDB entry 4h88 coloured by chain, front view.
PDB entry 4h88 coloured by chain, side view.
PDB entry 4h88 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein.
Sonati T, Reimann RR, Falsig J, Baral PK, O'Connor T, Hornemann S, Yaganoglu S, Li B, Herrmann US, Wieland B, Swayampakula M, Rahman MH, Das D, Kav N, Riek R, Liberski PP, James MN, Aguzzi A
Nature 501 102-6 (2013)
PMID: 23903654

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-209147 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 111 amino acids
Theoretical weight: 13.18 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P04925 (Residues: 120-230; Coverage: 48%)
Gene names: Prn-p, Prnp, Prp
Sequence domains: Prion/Doppel alpha-helical domain
POM1 FAB CHAIN H Chain: H
Molecule details ›
Chain: H
Length: 218 amino acids
Theoretical weight: 23.4 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
POM1 FAB CHAIN L Chain: L
Molecule details ›
Chain: L
Length: 213 amino acids
Theoretical weight: 23.51 KDa
Source organism: 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: 83.406Å b: 107.331Å c: 75.443Å
α: 90° β: 95.27° γ: 90°
R-values:
R R work R free
0.201 0.199 0.234
Expression system: Escherichia coli

Quick links

Citations

35 review citations

The immunobiology of prion diseases.
Aguzzi et al. (2013)
34 more

9 mentions without citation

Prion strains viewed through the lens of cryo-EM.
Manka et al. (2022)
8 more