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Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, NY 10021

Correspondence to Günter Blobel: blobel{at}rockefeller.edu

Abstract
Nucleocytoplasmic transport occurs through nuclear pore complexes (NPCs) whose complex architecture is generated from a set of only 30 proteins, termed nucleoporins. Here, we explore the domain structure of Nup133, a nucleoporin in a conserved NPC subcomplex that is crucial for NPC biogenesis and is believed to form part of the NPC scaffold. We show that human Nup133 contains two domains: a COOH-terminal domain responsible for its interaction with its subcomplex through Nup107; and an NH₂-terminal domain whose crystal structure reveals a seven-bladed ß-propeller. The surface properties and conservation of the Nup133 ß-propeller suggest it may mediate multiple interactions with other proteins. Other ß-propellers are predicted in a third of all nucleoporins. These and several other repeat-based motifs appear to be major elements of nucleoporins, indicating a level of structural repetition that may conceptually simplify the assembly and disassembly of this huge protein complex.

T.U. Schwartz's present address is Dept. of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.

Abbreviations used in this paper: CTD, COOH-terminal domain; NE, nuclear envelope; NPC, nuclear pore complex; NTD, NH₂-terminal domain.

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