› 4bs2

Solution NMR

NMR structure of human TDP-43 tandem RRMs in complex with UG-rich RNA

Released:
DOI: 10.2210/pdb4bs2/pdb
PDB entry 4bs2 coloured by chain, ensemble of 20 models, front view.
PDB entry 4bs2 coloured by chain, ensemble of 20 models, side view.
PDB entry 4bs2 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43.
Lukavsky PJ, Daujotyte D, Tollervey JR, Ule J, Stuani C, Buratti E, Baralle FE, Damberger FF, Allain FH
Nat Struct Mol Biol 20 1443-9 (2013)
PMID: 24240615

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171559 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
TAR DNA-binding protein 43 Chain: A
Molecule details ›
Chain: A
Length: 174 amino acids
Theoretical weight: 20 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13148 (Residues: 102-269; Coverage: 41%)
Gene names: TARDBP, TDP43
Sequence domains: RNA recognition motif
Structure domains: Alpha-Beta Plaits
5'-R(*GP*UP*GP*UP*GP*AP*AP*UP*GP*AP*AP*UP)-3' Chain: B
Molecule details ›
Chain: B
Length: 12 nucleotides
Theoretical weight: 3.88 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 92%
Refinement method: SIMULATED ANNEALING COMBINED WITH MOLECULAR DYNAMICS IN TORSION ANGLE SPACE
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

41 review citations

RNA-binding proteins with prion-like domains in health and disease.
Harrison et al. (2017)
40 more

42 mentions without citation

Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis.
Prasad et al. (2019)
41 more