› 6her

X-ray diffraction
1.2Å resolution

Mouse prion protein in complex with Nanobody 484

Released:
DOI: 10.2210/pdb6her/pdb
PDB entry 6her coloured by chain, front view.
PDB entry 6her coloured by chain, side view.
PDB entry 6her coloured by chain, top view.
Source organisms:
Primary publication:
Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion.
Abskharon R, Wang F, Wohlkonig A, Ruan J, Soror S, Giachin G, Pardon E, Zou W, Legname G, Ma J, Steyaert J
PLoS Pathog 15 e1008139 (2019)
PMID: 31815959

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-209152 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 110 amino acids
Theoretical weight: 12.92 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P04925 (Residues: 117-226; Coverage: 47%)
Gene names: Prn-p, Prnp, Prp
Sequence domains: Prion/Doppel alpha-helical domain
Nanobody 484 Chain: B
Molecule details ›
Chain: B
Length: 124 amino acids
Theoretical weight: 13.5 KDa
Source organism: Camelus dromedarius
Expression system: Escherichia coli

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 37.328Å b: 74.646Å c: 116.477Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.169 0.195
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Amyloidogenic Intrinsically Disordered Proteins: New Insights into Their Self-Assembly and Their Interaction with Membranes.
Scollo et al. (2020)
7 more