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. Author manuscript; available in PMC: 2012 Sep 10.
Published in final edited form as: Nat Struct Mol Biol. 2009 Apr 1;16(5):558–560. doi: 10.1038/nsmb.1586

Figure 2.

Figure 2

Positive cooperativity of substrate and Ran binding to CRM1. (a) The CRM1–SNUPN binary intermediate can accommodate RanGTP. Repeats H2–H7 of SNUPN-bound CRM1 were superimposed with H2–H7 of the CSE1–Kap60– RanGTP complex10 (PDB 1WA5). CRM1 and SNUPN are colored as in Figure 1 and RanGTP is in blue. CSE1 and Kap60 are omitted for clarity. (b) The electrostatic surface potential of SNUPN-bound CRM1 is shown with RanGTP from the superimposed CSE1–Kap60–Ran complex. The basic patch of Ran (residues 129–142) is in purple, the H9 loop sequence is shown and a dashed line indicates the disordered portion of this loop. (c) Pulldown assays with immobilized GST-NES of HIV1-REV and CRM1 proteins in the presence or absence of RanGTP and/or leptomycin B (LMB) were visualized by SDS-PAGE and Coomassie blue staining.