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Binding of CRM1 C-terminal helix variants to immobilized GST-PKI NES. A, whereas wild type CRM1 bound weakly to GST-PKI NES beads in pull-down experiments, all of the variant CRM1 constructs showed much stronger binding, consistent with the acidic residues at the extreme C terminus being critical. B shows the same proteins bound to the GST alone control resin.
