› 7dwv

Electron Microscopy
3.07Å resolution

Cryo-EM structure of amyloid fibril formed by familial prion disease-related mutation E196K

Released:
DOI: 10.2210/pdb7dwv/pdb
PDB entry 7dwv coloured by chain, front view.
PDB entry 7dwv coloured by chain, side view.
PDB entry 7dwv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Genetic prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM.
Wang LQ, Zhao K, Yuan HY, Li XN, Dang HB, Ma Y, Wang Q, Wang C, Sun Y, Chen J, Li D, Zhang D, Yin P, Liu C, Liang Y
OpenAccess logo Sci Adv 7 eabg9676 (2021)
PMID: 34516876
Related structures: EMD-30887

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137467 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 210 amino acids
Theoretical weight: 23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04156 (Residues: 23-231; Coverage: 91%)
Gene names: ALTPRP, PRIP, PRNP, PRP
Sequence domains: Prion/Doppel alpha-helical domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.07Å
Relevant EMDB volumes: EMD-30887
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Structural biology of ex vivo mammalian prions.
Artikis et al. (2022)
3 more

4 mentions without citation

Electrostatics in Computational Biophysics and Its Implications for Disease Effects.
Sun et al. (2022)
3 more