1W9C

Proteolytic fragment of CRM1 spanning six C-terminal HEAT repeats

Summary for 1W9C

• Entry DOI: 10.2210/pdb1w9c/pdb
• EMDB information: 1099
• Descriptor: CRM1 PROTEIN (2 entities in total)
• Functional Keywords: nuclear protein, exportin 1, nuclear export complex
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 72543.50

Authors

Petosa, C.,Schoehn, G.,Askjaer, P.,Bauer, U.,Moulin, M.,Steuerwald, U.,Soler-Lopez, M.,Baudin, F.,Mattaj, I.W.,Muller, C.W. (deposition date: 2004-10-08, release date: 2004-12-03, Last modification date: 2024-05-08)

Primary citation

Petosa, C.,Schoehn, G.,Askjaer, P.,Bauer, U.,Moulin, M.,Steuerwald, U.,Soler-Lopez, M.,Baudin, F.,Mattaj, I.W.,Muller, C.W.
Architecture of Crm1-Exportin 1 Suggests How Cooperativity is Achieved During Formation of a Nuclear Export Complex
Mol.Cell, 16:761-, 2004

PubMed Abstract: 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.

PubMed: 15574331
DOI: 10.1016/J.MOLCEL.2004.11.018

Experimental method

X-RAY DIFFRACTION (2.3 Å)