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TitleArchitecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex.
Journal, issue, pagesMol Cell, Vol. 16, Issue 5, Page 761-775, Year 2004
Publish dateDec 3, 2004
AuthorsCarlo Petosa / Guy Schoehn / Peter Askjaer / Ulrike Bauer / Martine Moulin / Ulrich Steuerwald / Montserrat Soler-López / Florence Baudin / Iain W Mattaj / Christoph W Müller /
PubMed AbstractCRM1/Exportin1 mediates the nuclear export of proteins bearing a leucine-rich nuclear export signal (NES) by forming a cooperative ternary complex with the NES-bearing substrate and the small GTPase ...CRM1/Exportin1 mediates the nuclear export of proteins bearing a leucine-rich nuclear export signal (NES) by forming a cooperative ternary complex with the NES-bearing substrate and the small GTPase Ran. We present a structural model of human CRM1 based on a combination of X-ray crystallography, homology modeling, and electron microscopy. The architecture of CRM1 resembles that of the import receptor transportin1, with 19 HEAT repeats and a large loop implicated in Ran binding. Residues critical for NES recognition are identified adjacent to the cysteine residue targeted by leptomycin B (LMB), a specific CRM1 inhibitor. We present evidence that a conformational change of the Ran binding loop accounts for the cooperativity of Ran- and substrate binding and for the selective enhancement of CRM1-mediated export by the cofactor RanBP3. Our findings indicate that a single architectural and mechanistic framework can explain the divergent effects of RanGTP on substrate binding by many import and export receptors.
External linksMol Cell / PubMed:15574331
MethodsEM (single particle) / X-ray diffraction
Resolution2.3 - 22.0 Å
Structure data

EMDB-1099:
Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex.
Method: EM (single particle) / Resolution: 22.0 Å

PDB-1w9c:
Proteolytic fragment of CRM1 spanning six C-terminal HEAT repeats
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsNUCLEAR PROTEIN / EXPORTIN 1 / NUCLEAR EXPORT COMPLEX

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