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. 2016 Jun 16;73(24):4685–4699. doi: 10.1007/s00018-016-2292-0

Fig. 1.

Fig. 1

CRM1 domains involved in NES binding and release. a Schematic representation of CRM1 protein showing the position of the NES-binding cleft, the loop connecting H9A and H9B helices (H9 loop) and the carboxy-terminal helix (C-helix) domains. b Detailed view of the NES-binding cleft on the molecular surface of CRM1 (Structure 3GJX, [4]). The image was produced using the UCSF Chimera package [53]. The pockets that serve as docking sites for NES hydrophobic residues Φ0–Φ4 are indicated on the left panel. The right panel depicts a classical leucine-rich NES peptide (ribbon representation, pink) with helix-loop conformation bound to the cleft