› 2n2c

Solution NMR

NMR Structure of TDP-43 prion-like hydrophobic helix in DPC

Released:
DOI: 10.2210/pdb2n2c/pdb
PDB entry 2n2c coloured by chain, ensemble of 6 models, front view.
PDB entry 2n2c coloured by chain, ensemble of 6 models, side view.
PDB entry 2n2c coloured by chain, ensemble of 6 models, top view.
Source organism: Homo sapiens
Primary publication:
ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.
Lim L, Wei Y, Lu Y, Song J
PLoS Biol 14 e1002338 (2016)
PMID: 26735904

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171557 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
TAR DNA-binding protein 43 Chain: A
Molecule details ›
Chain: A
Length: 43 amino acids
Theoretical weight: 4.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q13148 (Residues: 307-349; Coverage: 10%)
Gene names: TARDBP, TDP43
Sequence domains: TAR DNA-binding protein 43, C-terminal

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 62%
Refinement method: molecular dynamics
Expression system: Escherichia coli BL21

Quick links

Citations

30 review citations

Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease.
March et al. (2016)
29 more

3 mentions without citation

Structural Insights Into TDP-43 and Effects of Post-translational Modifications.
François-Moutal et al. (2019)
2 more