› 4hls

X-ray diffraction
1.45Å resolution

Crystal structure of mutant rabbit PRP 121-230 (S170N)

Released:
DOI: 10.2210/pdb4hls/pdb
PDB entry 4hls coloured by chain, front view.
PDB entry 4hls coloured by chain, side view.
PDB entry 4hls coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
N-terminal helix-cap in α-helix 2 modulates β-state misfolding in rabbit and hamster prion proteins.
Sweeting B, Brown E, Khan MQ, Chakrabartty A, Pai EF
OpenAccess logo PLoS One 8 e63047 (2013)
PMID: 23675452

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-188251 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 132 amino acids
Theoretical weight: 15.27 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q95211 (Residues: 119-229; Coverage: 50%)
Gene names: PRNP, PRP
Sequence domains: Prion/Doppel alpha-helical domain

Ligands and Environments

3 bound ligands:
Ligand CL 2 x CL
Ligand NA 6 x NA
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 29.52Å b: 86.08Å c: 86.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.146 0.18
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

In Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding.
Eraña et al. (2017)
8 more

1 mention without citation

On the Dependence of Prion and Amyloid Structure on the Folding Environment.
Roterman et al. (2021)