Electrostatic Interactions Involving the Extreme C Terminus of Nuclear Export Factor CRM1 Modulate Its Affinity for Cargo*
The toroid-shaped nuclear protein export factor CRM1 is constructed from 21 tandem HEAT repeats, each of which contains an inner (B) and outer (A) α-helix joined by loops. Proteins targeted for export have a nuclear export signal (NES) that binds between the A-helices of HEAT repeats 11 and 12 on th...
| Main Authors: | , , , |
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| Format: | Online |
| Language: | English |
| Published: |
American Society for Biochemistry and Molecular Biology
2011
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3190738/ |