Abstract：
:Nup98 is a component of the nuclear pore that plays its primary role in the export of RNAs. Nup98 is expressed in two forms, derived from alternate mRNA splicing. Both forms are processed into two peptides through autoproteolysis mediated by the C-terminal domain of hNup98. The three-dimensional structure of the C-terminal domain reveals a novel protein fold, and thus a new class of autocatalytic proteases. The structure further reveals that the suggested nucleoporin RNA binding motif is unlikely to bind to RNA. The C terminus also contains sequences that target hNup98 to the nuclear pore complex. Noncovalent interactions between the C-terminal domain and the cleaved peptide tail are visible and suggest a model for cleavage-dependent targeting of hNup98 to the nuclear pore.
journal_name
Mol Celljournal_title
Molecular cellauthors
Hodel AE,Hodel MR,Griffis ER,Hennig KA,Ratner GA,Xu S,Powers MAdoi
10.1016/s1097-2765(02)00589-0subject
Has Abstractpub_date
2002-08-01 00:00:00pages
347-58issue
2eissn
1097-2765issn
1097-4164pii
S1097-2765(02)00589-0journal_volume
10pub_type
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