› 4n9o

X-ray diffraction
1.5Å resolution

Probing the N-terminal beta-sheet conversion in the crystal structure of the human prion protein bound to a Nanobody

Released:
DOI: 10.2210/pdb4n9o/pdb
PDB entry 4n9o coloured by chain, front view.
PDB entry 4n9o coloured by chain, side view.
PDB entry 4n9o coloured by chain, top view.
Source organisms:
Primary publication:
Probing the N-terminal β-sheet conversion in the crystal structure of the human prion protein bound to a nanobody.
Abskharon RN, Giachin G, Wohlkonig A, Soror SH, Pardon E, Legname G, Steyaert J
J Am Chem Soc 136 937-44 (2014)
PMID: 24400836

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-208988 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 142 amino acids
Theoretical weight: 16.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04156 (Residues: 90-231; Coverage: 62%)
Gene names: ALTPRP, PRIP, PRNP, PRP
Sequence domains: Prion/Doppel alpha-helical domain
Nanobody Nb484 Chain: B
Molecule details ›
Chain: B
Length: 130 amino acids
Theoretical weight: 14.25 KDa
Source organism: Lama glama
Expression system: Escherichia coli
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: C2
Unit cell:
a: 131.857Å b: 45.781Å c: 45.092Å
α: 90° β: 96.23° γ: 90°
R-values:
R R work R free
0.151 0.15 0.184
Expression system: Escherichia coli

Quick links

Citations

25 review citations

Nanobody-based products as research and diagnostic tools.
De Meyer et al. (2014)
24 more

2 mentions without citation

Met/Val129 polymorphism of the full-length human prion protein dictates distinct pathways of amyloid formation.
Pauly et al. (2022)
1 more