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The nuclear envelope creates distinct nuclear and cytoplasmic compartments in eukaryotic cells.
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human Nup133 contains two domains: a COOH-terminal domain responsible for its interaction with its subcomplex through Nup107 (Montrer NUP107 Kits ELISA); and an NH2-terminal domain whose crystal structure reveals a seven-bladed beta-propeller.
When complexed with NUP107 (Montrer NUP107 Kits ELISA), this complex will give the first insights into the protein-protein interactions within a core module of the nuclear pore complex.
The significant topological differences between Nup107 and Nup133 suggest that helical nucleoporin domains of the nuclear pore complex scaffold fall in different classes and fulfill largely nonredundant functions.
Data present crystal structures of yNup170(979-1502) and hNup107(658-925) x hNup133(517-1156), and conservation of domain arrangement and of tertiary structure suggests that Nup157/170 and Nup133 derived from a common ancestor.
The nuclear envelope creates distinct nuclear and cytoplasmic compartments in eukaryotic cells. It consists of two concentric membranes perforated by nuclear pores, large protein complexes that form aqueous channels to regulate the flow of macromolecules between the nucleus and the cytoplasm. These complexes are composed of at least 100 different polypeptide subunits, many of which belong to the nucleoporin family. The nucleoporin protein encoded by this gene displays evolutionarily conserved interactions with other nucleoporins. This protein, which localizes to both sides of the nuclear pore complex at interphase, remains associated with the complex during mitosis and is targeted at early stages to the reforming nuclear envelope. This protein also localizes to kinetochores of mitotic cells.
, nuclear pore complex protein Nup133-like
, 133 kDa nucleoporin
, nuclear pore complex protein Nup133
, nucleoporin Nup133