期刊
JOURNAL OF CELL BIOLOGY
卷 167, 期 4, 页码 591-597出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200408109
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Nucleocytoplasmic transport occurs through nuclear pore complexes (NPCs) whose complex architecture is generated from a set of only similar to30 proteins, termed nucleoporins. Here, we explore the domain structure of Nup133, a nucleoporin in a conserved NPC subcomplex that is crucial for l biogenesis and is believed to form part of the NPC scaffold. We show that human Nul 33 contains two domains: a COOH-terminal domain responsible for its interaction with its subcomplex through Nul and an NH2-terminal domain whose crystal structure reveals a seven-bladed beta-propeller. The surface properties and conservation of the Nul beta-propeller suggest it may mediate multiple interactions with other proteins. Other beta-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.
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