› 3heq

X-ray diffraction
1.8Å resolution

Human prion protein variant D178N with M129

Released:
DOI: 10.2210/pdb3heq/pdb
PDB entry 3heq coloured by chain, front view.
PDB entry 3heq coloured by chain, side view.
PDB entry 3heq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conformational diversity in prion protein variants influences intermolecular beta-sheet formation.
Lee S, Antony L, Hartmann R, Knaus KJ, Surewicz K, Surewicz WK, Yee VC
EMBO J 29 251-62 (2010)
PMID: 19927125

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137455 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chains: A, B
Molecule details ›
Chains: A, B
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
Structure domains: Prion/Doppel protein, beta-ribbon domain

Ligands and Environments

1 bound ligand:
Ligand CD 2 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P43212
Unit cell:
a: 57.489Å b: 57.489Å c: 168.013Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.206 0.232
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Molecular biology and pathology of prion strains in sporadic human prion diseases.
Gambetti et al. (2011)
7 more

4 mentions without citation

Conformational diversity in prion protein variants influences intermolecular beta-sheet formation.
Lee et al. (2010)
3 more