› 4bsm

X-ray diffraction
4.5Å resolution

Crystal structure of the Nuclear Export Receptor CRM1 (exportin-1) lacking the C-terminal helical extension at 4.5A

Released:
DOI: 10.2210/pdb4bsm/pdb
PDB entry 4bsm coloured by chain, front view.
PDB entry 4bsm coloured by chain, side view.
PDB entry 4bsm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of a truncation mutant of the nuclear export factor CRM1 provides insights into the auto-inhibitory role of its C-terminal helix.
Dian C, Bernaudat F, Langer K, Oliva MF, Fornerod M, Schoehn G, Müller CW, Petosa C
Structure 21 1338-49 (2013)
PMID: 23850454

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127255 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exportin-1 Chain: A
Molecule details ›
Chain: A
Length: 1032 amino acids
Theoretical weight: 118.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O14980 (Residues: 1-1032; Coverage: 96%)
Gene names: CRM1, XPO1
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2221
Unit cell:
a: 148.64Å b: 248.33Å c: 107.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.229 0.269
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Atomic basis of CRM1-cargo recognition, release and inhibition.
Fung et al. (2014)
5 more

2 mentions without citation

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