› 8a9l

Electron Microscopy
2.16Å resolution

Cryo-EM structure of alpha-synuclein filaments from Parkinson's disease and dementia with Lewy bodies

Released:
DOI: 10.2210/pdb8a9l/pdb
PDB entry 8a9l coloured by chain, front view.
PDB entry 8a9l coloured by chain, side view.
PDB entry 8a9l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of α-synuclein filaments from human brains with Lewy pathology.
Yang Y, Shi Y, Schweighauser M, Zhang X, Kotecha A, Murzin AG, Garringer HJ, Cullinane PW, Saito Y, Foroud T, Warner TT, Hasegawa K, Vidal R, Murayama S, Revesz T, Ghetti B, Hasegawa M, Lashley T, Scheres SHW, Goedert M
Nature (2022)
PMID: 36108674
Related structures: EMD-15285

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero nonamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153508 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Alpha-synuclein Chain: A
Molecule details ›
Chain: A
Length: 140 amino acids
Theoretical weight: 14.48 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P37840 (Residues: 1-140; Coverage: 100%)
Gene names: NACP, PARK1, SNCA
Sequence domains: Synuclein
Unknown fragment Chain: B
Molecule details ›
Chain: B
Length: 9 amino acids
Theoretical weight: 784 Da
Source organism: Homo sapiens
Unknown fragment Chain: C
Molecule details ›
Chain: C
Length: 7 amino acids
Theoretical weight: 628 Da
Source organism: Homo sapiens

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.16Å
Relevant EMDB volumes: EMD-15285

Quick links

Citations

18 review citations

Monitoring α-synuclein aggregation.
Estaun-Panzano et al. (2023)
17 more

6 mentions without citation

Effects of Mutations and Post-Translational Modifications on α-Synuclein In Vitro Aggregation.
Pancoe et al. (2022)
5 more