› 2w9e

X-ray diffraction
2.9Å resolution

Structure of ICSM 18 (anti-Prp therapeutic antibody) Fab fragment complexed with human Prp fragment 119-231

Released:
DOI: 10.2210/pdb2w9e/pdb
PDB entry 2w9e coloured by chain, front view.
PDB entry 2w9e coloured by chain, side view.
PDB entry 2w9e coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of human prion protein bound to a therapeutic antibody.
Antonyuk SV, Trevitt CR, Strange RW, Jackson GS, Sangar D, Batchelor M, Cooper S, Fraser C, Jones S, Georgiou T, Khalili-Shirazi A, Clarke AR, Hasnain SS, Collinge J
Proc Natl Acad Sci U S A 106 2554-8 (2009)
PMID: 19204296

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-208985 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 113 amino acids
Theoretical weight: 13.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04156 (Residues: 119-231; Coverage: 49%)
Gene names: ALTPRP, PRIP, PRNP, PRP
Sequence domains: Prion/Doppel alpha-helical domain
Structure domains: Prion/Doppel protein, beta-ribbon domain
ICSM 18-ANTI-PRP THERAPEUTIC FAB HEAVY CHAIN Chain: H
Molecule details ›
Chain: H
Length: 215 amino acids
Theoretical weight: 23.05 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
ICSM 18-ANTI-PRP THERAPEUTIC FAB LIGHT CHAIN Chain: L
Molecule details ›
Chain: L
Length: 212 amino acids
Theoretical weight: 23.28 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P6322
Unit cell:
a: 126.149Å b: 126.149Å c: 134.126Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.207 0.269
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Prions.
Colby et al. (2011)
9 more

16 mentions without citation

The consequences of pathogenic mutations to the human prion protein.
van der Kamp et al. (2009)
15 more