› 1i4m

X-ray diffraction
2Å resolution

Crystal structure of the human prion protein reveals a mechanism for oligomerization

Released:
DOI: 10.2210/pdb1i4m/pdb
PDB entry 1i4m coloured by chain, front view.
PDB entry 1i4m coloured by chain, side view.
PDB entry 1i4m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the human prion protein reveals a mechanism for oligomerization.
Knaus KJ, Morillas M, Swietnicki W, Malone M, Surewicz WK, Yee VC
Nat Struct Biol 8 770-4 (2001)
PMID: 11524679

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137464 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 108 amino acids
Theoretical weight: 12.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04156 (Residues: 119-226; Coverage: 47%)
Gene names: ALTPRP, PRIP, PRNP, PRP
Sequence domains: Prion/Doppel alpha-helical domain
Structure domains: Prion/Doppel protein, beta-ribbon domain

Ligands and Environments

2 bound ligands:
Ligand CD 2 x CD
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2221
Unit cell:
a: 85.441Å b: 85.707Å c: 40.501Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.206 0.253
Expression system: Escherichia coli

Quick links

Citations

64 review citations

Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders.
Caughey et al. (2003)
63 more

26 mentions without citation

Protein acrobatics in pairs--dimerization via domain swapping.
Gronenborn AM. (2009)
25 more