› 4b18

X-ray diffraction
2.52Å resolution

The crystal structure of human Importin alpha 5 with TERT NLS peptide

Released:
DOI: 10.2210/pdb4b18/pdb
PDB entry 4b18 coloured by chain, front view.
PDB entry 4b18 coloured by chain, side view.
PDB entry 4b18 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Akt-mediated phosphorylation increases the binding affinity of hTERT for importin α to promote nuclear translocation.
Jeong SA, Kim K, Lee JH, Cha JS, Khadka P, Cho HS, Chung IK
J Cell Sci 128 2287-301 (2015)
PMID: 25999477

Function and Biology Details

Reaction catalysed: 
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127091 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Importin subunit alpha-5, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 447 amino acids
Theoretical weight: 49.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P52294 (Residues: 66-512; Coverage: 83%)
Gene names: KPNA1, RCH2
Sequence domains:
Structure domains: Leucine-rich Repeat Variant
Telomerase reverse transcriptase Chain: B
Molecule details ›
Chain: B
Length: 20 amino acids
Theoretical weight: 2.28 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: O14746 (Residues: 222-240; Coverage: 2%)
Gene names: EST2, TCS1, TERT, TRT

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: C2
Unit cell:
a: 159.723Å b: 59.916Å c: 69.331Å
α: 90° β: 96.29° γ: 90°
R-values:
R R work R free
0.201 0.198 0.253
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

8 review citations

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

4 mentions without citation

Diversification of importin-α isoforms in cellular trafficking and disease states.
Pumroy et al. (2015)
3 more