Structure of importin-β bound to the IBB domain of importin-α

Gino Cingolani, Carlo Petosa, Karsten Weis and Christoph W. Müller ()
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Gino Cingolani: European Molecular Biology Laboratory (EMBL)
Carlo Petosa: European Molecular Biology Laboratory (EMBL)
Karsten Weis: University of California
Christoph W. Müller: European Molecular Biology Laboratory (EMBL)

Nature, 1999, vol. 399, issue 6733, 221-229

Abstract: Abstract Cytosolic proteins bearing a classical nuclear localization signal enter the nucleus bound to a heterodimer of importin-α and importin-β (also called karyopherin-α and -β). The formation of this heterodimer involves the importin-β-binding (IBB) domain of importin-α, a highly basic amino-terminal region of roughly 40 amino-acid residues. Here we report the crystal structure of human importin-β bound to the IBB domain of importin-α, determined at 2.5 Å and 2.3 Å resolution in two crystal forms. Importin-β consists of 19 tandemly repeated HEAT motifs and wraps intimately around the IBB domain. The association involves two separate regions of importin-β, recognizing structurally distinct parts of the IBB domain: an amino-terminal extended moiety and a carboxy-terminal helix. The structure indicates that significant conformational changes occur when importin-β binds or releases the IBB domain domain and suggests how dissociation of the importin-α/β heterodimer may be achieved upon nuclear entry.

Date: 1999
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DOI: 10.1038/20367

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