› 1w9c

X-ray diffraction
2.3Å resolution

Proteolytic fragment of CRM1 spanning six C-terminal HEAT repeats

Released:
DOI: 10.2210/pdb1w9c/pdb
PDB entry 1w9c coloured by chain, front view.
PDB entry 1w9c coloured by chain, side view.
PDB entry 1w9c coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex.
Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, Steuerwald U, Soler-López M, Baudin F, Mattaj IW, Müller CW
Mol Cell 16 761-75 (2004)
PMID: 15574331

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127260 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exportin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 321 amino acids
Theoretical weight: 36.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O14980 (Residues: 707-1027; Coverage: 30%)
Gene names: CRM1, XPO1
Sequence domains: CRM1 C terminal
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: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 118.87Å b: 62.87Å c: 114.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.229 0.277
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Mechanisms of receptor-mediated nuclear import and nuclear export.
Pemberton et al. (2005)
19 more

5 mentions without citation

Allosteric control of the exportin CRM1 unraveled by crystal structure analysis.
Monecke et al. (2014)
4 more