Structural basis of the nic96 subcomplex organization in the nuclear pore channel.

Nic96 is a conserved nucleoporin that recruits the Nsp1-Nup49-Nup57 complex, a module with Phe-Gly (FG) repeats, to the central transport channel of the nuclear pore complex (NPC). Nic96 binds the Nsp1 complex via its N domain and assembles into the NPC framework via its central and C domain. Here, we ...
report the crystal structure of a large structural nucleoporin, Nic96 without its N domain (Nic96DeltaN). Nic96DeltaN is composed of three domains and is a straight molecule that--although almost entirely helical--exhibits strong deviations from the predicted alpha-solenoid fold. The missing N domain projects midway from the Nic96 molecule, indicating how the Nsp1 complex might be located with respect to the rod-like Nic96. Notably, Nic96DeltaN binds in vitro to FG repeats of the Nsp1 complex. These data suggest a model of how Nic96 could organize a transport module with coiled-coil domains and FG repeats in the central pore channel.
Mesh Terms:
Calcium-Binding Proteins, Crystallography, X-Ray, Membrane Proteins, Microscopy, Electron, Models, Molecular, Multiprotein Complexes, Nuclear Pore, Nuclear Pore Complex Proteins, Nuclear Proteins, Point Mutation, Protein Conformation, Protein Interaction Mapping, Protein Structure, Tertiary, Recombinant Fusion Proteins, Repetitive Sequences, Amino Acid, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Structure-Activity Relationship
Mol. Cell
Date: Jan. 18, 2008
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