› 6lni

Electron Microscopy
2.7Å resolution

Cryo-EM structure of amyloid fibril formed by full-length human prion protein

Released:
DOI: 10.2210/pdb6lni/pdb
PDB entry 6lni coloured by chain, front view.
PDB entry 6lni coloured by chain, side view.
PDB entry 6lni coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cryo-EM structure of an amyloid fibril formed by full-length human prion protein.
Wang LQ, Zhao K, Yuan HY, Wang Q, Guan Z, Tao J, Li XN, Sun Y, Yi CW, Chen J, Li D, Zhang D, Yin P, Liu C, Liang Y
Nat Struct Mol Biol 27 598-602 (2020)
PMID: 32514176
Related structures: EMD-0931

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137462 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
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: 2.702Å
Relevant EMDB volumes: EMD-0931
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins.
Bianchi et al. (2020)
17 more

9 mentions without citation

Modeling PrPSc Generation Through Deformed Templating.
Spagnolli et al. (2020)
8 more