1ko6
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ko6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ko6 OCA], [http://www.ebi.ac.uk/pdbsum/1ko6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ko6 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Leukemia, lymphycytic, acute T-cell OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601021 601021]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: nucleoporin]] | [[Category: nucleoporin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:51:14 2008'' |
Revision as of 18:51, 30 March 2008
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| , resolution 3.00Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of C-terminal Autoproteolytic Domain of Nucleoporin Nup98
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.
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
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