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Schrader, N, Stelter, P, Flemming, D, Kunze, R, Hurt, E and Vetter, IR (2008) Structural basis of the nic96 subcomplex organization in the nuclear pore channel. Mol. Cell 29:46-55


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.


PubMed Online version:10.1016/j.molcel.2007.10.022


Calcium-Binding Proteins/chemistry; Calcium-Binding Proteins/ultrastructure; Crystallography, X-Ray; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/ultrastructure; Microscopy, Electron; Models, Molecular; Multiprotein Complexes/chemistry; Multiprotein Complexes/ultrastructure; Nuclear Pore/chemistry; Nuclear Pore/ultrastructure; Nuclear Pore Complex Proteins/chemistry; Nuclear Pore Complex Proteins/ultrastructure; Nuclear Proteins/chemistry; Nuclear Proteins/genetics; Nuclear Proteins/ultrastructure; Point Mutation; Protein Conformation; Protein Interaction Mapping; Protein Structure, Tertiary; Recombinant Fusion Proteins/chemistry; Repetitive Sequences, Amino Acid; Saccharomyces cerevisiae/chemistry; Saccharomyces cerevisiae/ultrastructure; Saccharomyces cerevisiae Proteins/chemistry; Saccharomyces cerevisiae Proteins/genetics; Saccharomyces cerevisiae Proteins/ultrastructure; Structure-Activity Relationship



Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status



GO:0017056: structural constituent of nuclear pore

ECO:0000315: mutant phenotype evidence used in manual assertion


Seeded From UniProt


See also


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