› 6xyq

Electron Microscopy
3.09Å resolution

Multiple system atrophy Type II-2 alpha-synuclein filament

Released:
DOI: 10.2210/pdb6xyq/pdb
PDB entry 6xyq coloured by chain, front view.
PDB entry 6xyq coloured by chain, side view.
PDB entry 6xyq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of α-synuclein filaments from multiple system atrophy.
Schweighauser M, Shi Y, Tarutani A, Kametani F, Murzin AG, Ghetti B, Matsubara T, Tomita T, Ando T, Hasegawa K, Murayama S, Yoshida M, Hasegawa M, Scheres SHW, Goedert M
Nature 585 464-469 (2020)
PMID: 32461689
Related structures: EMD-10652

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-153502 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-synuclein 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: 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

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.09Å
Relevant EMDB volumes: EMD-10652

Quick links

Citations

111 review citations

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.
Nguyen et al. (2021)
110 more

8 mentions without citation

Crosstalk Between Alpha-Synuclein and Other Human and Non-Human Amyloidogenic Proteins: Consequences for Amyloid Formation in Parkinson's Disease.
Werner et al. (2020)
7 more