Structural studies of the interactions between the nuclear protein export factor CRM1 and its partners
To investigate the position of the C-terminal helix in unbound CRM1/Xpo1p, SAXS was used to compare the solution conformations of CRM1/Xpo1p to the known crystal structures. This study indicated that the C-terminal helix is likely to lie across the toroid when neither RanGTP nor NES cargo is bound....
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University of Cambridge
2010
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| Online Access: | http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.599160 |