› 4ril

Electron crystallography
1.43Å resolution

Structure of the amyloid forming segment, GAVVTGVTAVA, from the NAC domain of Parkinson's disease protein alpha-synuclein, residues 68-78, determined by electron diffraction

Released:
DOI: 10.2210/pdb4ril/pdb
PDB 4ril coloured by chain and viewed from the front.
PDB 4ril coloured by chain and viewed from the side.
PDB 4ril coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Structure of the toxic core of α-synuclein from invisible crystals.
Rodriguez JA, Ivanova MI, Sawaya MR, Cascio D, Reyes FE, Shi D, Sangwan S, Guenther EL, Johnson LM, Zhang M, Jiang L, Arbing MA, Nannenga BL, Hattne J, Whitelegge J, Brewster AS, Messerschmidt M, Boutet S, Sauter NK, Gonen T, Eisenberg DS
Nature 525 486-90 (2015)
PMID: 26352473
Related structures: EMD-3028

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-synuclein Chain: A
Molecule details ›
Chain: A
Length: 11 amino acids
Theoretical weight: 944 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P37840 (Residues: 68-78; Coverage: 8%)
Gene names: NACP, PARK1, SNCA

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 1.43Å
Relevant EMDB volumes: EMD-3028
Expression system: Not provided

Quick links

Citations

79 review citations

Amyloid-Like Aggregation in Diseases and Biomaterials: Osmosis of Structural Information.
Balasco et al. (2021)
78 more

1 mention without citation

Energetics of cosolvent effect on peptide aggregation.
Matubayasi et al. (2019)