› 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 entry 4ril coloured by chain, front view.
PDB entry 4ril coloured by chain, side view.
PDB entry 4ril coloured by chain, top view.
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)
Assembly name:
PDBe Complex ID:
PDB-CPX-153502 (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

120 review citations

Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.
Chiti et al. (2017)
119 more

12 mentions without citation

Versatile Structures of α-Synuclein.
Wang et al. (2016)
11 more