› 3nhd

X-ray diffraction
1.92Å resolution

GYVLGS segment 127-132 from human prion with V129

Released:
DOI: 10.2210/pdb3nhd/pdb
PDB entry 3nhd coloured by chain, front view.
PDB entry 3nhd coloured by chain, side view.
PDB entry 3nhd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease.
Apostol MI, Sawaya MR, Cascio D, Eisenberg D
J Biol Chem 285 29671-5 (2010)
PMID: 20685658

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137463 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 6 amino acids
Theoretical weight: 595 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P04156 (Residues: 127-132; Coverage: 3%)
Gene names: ALTPRP, PRIP, PRNP, PRP

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21212
Unit cell:
a: 41.173Å b: 18.959Å c: 9.585Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.203 0.261
Expression system: Not provided

Quick links

Citations

11 review citations

The amyloid state of proteins in human diseases.
Eisenberg et al. (2012)
10 more

5 mentions without citation

Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease.
Apostol et al. (2010)
4 more