1ko6
From Proteopedia
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Crystal Structure of C-terminal Autoproteolytic Domain of Nucleoporin Nup98
Contents |
Overview
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.
Disease
Known disease associated with this structure: Leukemia, lymphycytic, acute T-cell OMIM:[601021]
About this Structure
1KO6 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98., Hodel AE, Hodel MR, Griffis ER, Hennig KA, Ratner GA, Xu S, Powers MA, Mol Cell. 2002 Aug;10(2):347-58. PMID:12191480
Page seeded by OCA on Mon Nov 12 17:52:55 2007
