3TKN: Structure Of The Nup82-Nup159-Nup98 Heterotrimer

The cytoplasmic filament nucleoporins of the nuclear pore complex (NPC) are critically involved in nuclear export and remodeling of mRNA ribonucleoprotein particles and are associated with various human malignancies. Here, we report the crystal structure of the Nup98 C-terminal autoproteolytic domain, frequently missing from leukemogenic forms of the protein, in complex with the N-terminal domain of Nup82 and the C-terminal tail fragment of Nup159. The Nup82 beta propeller serves as a noncooperative binding platform for both binding partners. Interaction of Nup98 with Nup82 occurs through a reciprocal exchange of loop structures. Strikingly, the same Nup98 groove promiscuously interacts with Nup82 and Nup96 in a mutually excusive fashion. Simultaneous disruption of both Nup82 interactions in yeast causes severe defects in mRNA export, while the severing of a single interaction is tolerated. Thus, the cytoplasmic filament network of the NPC is robust, consistent with its essential function in nucleocytoplasmic transport.
PDB ID: 3TKNDownload
MMDB ID: 98672
PDB Deposition Date: 2011/8/28
Updated in MMDB: 2012/06
Experimental Method:
x-ray diffraction
Resolution: 3.4  Å
Source Organism:
Mus musculus
Similar Structures:
Biological Unit for 3TKN: trimeric; determined by author and by software (PISA)
Molecular Components in 3TKN
Label Count Molecule
Proteins (3 molecules)
Nucleoporin Nup82(Gene symbol: NUP82)
Molecule annotation
Nucleoporin Nup159(Gene symbol: NUP159)
Molecule annotation
Nucleoporin 98(Gene symbol: Nup98)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB