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Published Online April 23, 2009
Science DOI: 10.1126/science.1173388

Reports

Submitted on March 11, 2009
Accepted on April 9, 2009

Crystal Structure of the Nuclear Export Receptor CRM1 in Complex with Snurportin1 and RanGTP

Thomas Monecke 1{dagger}, Thomas Güttler 2{dagger}, Piotr Neumann 1, Achim Dickmanns 1, Dirk Görlich 2*, Ralf Ficner 1

1 Abteilung für Molekulare Strukturbiologie, Institut für Mikrobiologie und Genetik, GZMB, Georg-August-Universität Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany
2 Abteilung Zelluläre Logistik, Max-Planck-Institut für biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen, Germany.

* To whom correspondence should be addressed.
Dirk Görlich , E-mail: goerlich{at}mpibpc.mpg.de

{dagger}These authors contributed equally to this work.

CRM1 mediates nuclear export of numerous unrelated cargoes, which may carry a short leucine-rich nuclear export signal or export signatures that include folded domains. How CRM1 recognizes such a variety of cargoes has been unknown. Here, we present the crystal structure of the snurportin1-CRM1-RanGTP export complex at 2.5 Å resolution. Snurportin1 is a nuclear import adapter for cytoplasmically assembled, m3G-capped spliceosomal U snRNPs. The structure shows how CRM1 can specifically return the cargo-free form of snurportin1 to the cytoplasm. The extensive contact area includes five hydrophobic residues at the snurportin1 N terminus that dock into a hydrophobic cleft of CRM1, as well as numerous hydrophilic contacts of CRM1 to m3G cap-binding domain and C-terminal residues of snurportin1. The structure suggests that RanGTP promotes cargo-binding to CRM1 solely through long-range conformational changes in the exportin.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)