› 3nhd

X-ray diffraction
1.92Å resolution

GYVLGS segment 127-132 from human prion with V129

Released:
DOI: 10.2210/pdb3nhd/pdb
PDB 3nhd coloured by chain and viewed from the front.
PDB 3nhd coloured by chain and viewed from the side.
PDB 3nhd coloured by chain and viewed from the top.
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
OpenAccess logo 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)
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

Structural mechanisms of oligomer and amyloid fibril formation by the prion protein.
Sengupta et al. (2018)
10 more

3 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)
2 more