5DIF: Crystal Structure Of Cpeb4 Nes Peptide In Complex With Crm1-ran-ranbp1

Citation:
Abstract
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). 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.
PDB ID: 5DIFDownload
MMDB ID: 132733
PDB Deposition Date: 2015/8/31
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.09  Å
Source Organism:
Saccharomyces cerevisiae S288C
Similar Structures:
Biological Unit for 5DIF: tetrameric; determined by author and by software (PISA)
Molecular Components in 5DIF
Label Count Molecule
Proteins (4 molecules)
1
Gtp-binding Nuclear Protein RAN(Gene symbol: RAN)
Molecule annotation
1
Ran-specific Gtpase-activating Protein 1(Gene symbol: YRB1)
Molecule annotation
1
Exportin-1(Gene symbol: CRM1)
Molecule annotation
1
Cytoplasmic Polyadenylation Element-binding Protein 4
Molecule annotation
Chemicals (10 molecules)
1
1
2
1
3
7
4
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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