› 3oqs

X-ray diffraction
2Å resolution

Crystal structure of importin-alpha bound to a CLIC4 NLS peptide

Released:
DOI: 10.2210/pdb3oqs/pdb
PDB entry 3oqs coloured by chain, front view.
PDB entry 3oqs coloured by chain, side view.
PDB entry 3oqs coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of importin-α bound to a peptide bearing the nuclear localisation signal from chloride intracellular channel protein 4.
Mynott AV, Harrop SJ, Brown LJ, Breit SN, Kobe B, Curmi PM
FEBS J 278 1662-75 (2011)
PMID: 21388519

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156539 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chloride intracellular channel protein 4 Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.21 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9Y696 (Residues: 198-207; Coverage: 4%)
Gene name: CLIC4
Importin subunit alpha-1 Chain: A
Molecule details ›
Chain: A
Length: 510 amino acids
Theoretical weight: 55.33 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P52293 (Residues: 70-529; Coverage: 87%)
Gene names: Kpna2, Rch1
Sequence domains:
Structure domains: Leucine-rich Repeat Variant

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P212121
Unit cell:
a: 78.594Å b: 89.558Å c: 100.083Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.237
Expression systems:
  • Not provided
  • Escherichia coli

Quick links

Citations

4 review citations

Structural Biology and Regulation of Protein Import into the Nucleus.
Christie et al. (2016)
3 more

5 mentions without citation

The C-terminal 18 Amino Acid Region of Dengue Virus NS5 Regulates its Subcellular Localization and Contains a Conserved Arginine Residue Essential for Infectious Virus Production.
Tay et al. (2016)
4 more