Structural determinants of nuclear export signal orientation in binding to exportin CRM1 [electronic resource].
- Washington, D.C. : United States. Dept. of Energy, 2015.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy
- Physical Description:
- Article numbers e10,034 : digital, PDF file
- Additional Creators:
- Argonne National Laboratory
United States. Department of Energy
United States. Department of Energy. Office of Scientific and Technical Information
- The Chromosome Region of Maintenance 1 (CRM1) protein mediates nuclear export of hundreds of proteins through recognition of their nuclear export signals (NESs), which are highly variable in sequence and structure. The plasticity of the CRM1-NES interaction is not well understood, as there are many NES sequences that seem incompatible with structures of the NES-bound CRM1 groove. Crystal structures of CRM1 bound to two different NESs with unusual sequences showed the NES peptides binding the CRM1 groove in the opposite orientation (minus) to that of previously studied NESs (plus). A comparison of minus and plus NESs identified structural and sequence determinants for NES orientation. The binding of NESs to CRM1 in both orientations results in a large expansion in NES consensus patterns and therefore a corresponding expansion of potential NESs in the proteome.
- Published through SciTech Connect.
eLife 4 ISSN 2050-084X AM
Fung, Ho; Fu, Szu; Brautigam, Chad; Chook, Yuh.
- Funding Information:
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