› 2mdr

Solution NMR

Solution structure of the third double-stranded RNA-binding domain (dsRBD3) of human adenosine-deaminase ADAR1

Released:
DOI: 10.2210/pdb2mdr/pdb
PDB entry 2mdr coloured by chain, ensemble of 20 models, front view.
PDB entry 2mdr coloured by chain, ensemble of 20 models, side view.
PDB entry 2mdr coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1.
Barraud P, Banerjee S, Mohamed WI, Jantsch MF, Allain FH
Proc Natl Acad Sci U S A 111 E1852-61 (2014)
PMID: 24753571

Function and Biology Details

Reaction catalysed: 
Adenine in double-stranded RNA + H(2)O = hypoxanthine in double-stranded RNA + NH(3)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157286 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Double-stranded RNA-specific adenosine deaminase Chain: A
Molecule details ›
Chain: A
Length: 113 amino acids
Theoretical weight: 12.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55265 (Residues: 708-801; Coverage: 8%)
Gene names: ADAR, ADAR1, DSRAD, G1P1, IFI4
Sequence domains: Double-stranded RNA binding motif
Structure domains: Double Stranded RNA Binding Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 84%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

20 review citations

A-to-I editing of coding and non-coding RNAs by ADARs.
Nishikura K. (2016)
19 more

5 mentions without citation

'Black sheep' that don't leave the double-stranded RNA-binding domain fold.
Gleghorn et al. (2014)
4 more