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| | <StructureSection load='3tkn' size='340' side='right'caption='[[3tkn]], [[Resolution|resolution]] 3.40Å' scene=''> | | <StructureSection load='3tkn' size='340' side='right'caption='[[3tkn]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3tkn]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TKN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3tkn]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TKN FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HRB187, J1135, NUP82, YJL061W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), NUP158, NUP159, RAT7, YIL115C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), Nup98 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4Å</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tkn OCA], [https://pdbe.org/3tkn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tkn RCSB], [https://www.ebi.ac.uk/pdbsum/3tkn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tkn ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tkn OCA], [https://pdbe.org/3tkn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tkn RCSB], [https://www.ebi.ac.uk/pdbsum/3tkn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tkn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/NUP82_YEAST NUP82_YEAST]] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved as part of the NUP82-NUP159-NSP1 subcomplex in nuclear mRNA and pre-ribosome export by acting as a linker tethering nucleoporins that are directly involved in nuclear transport to the NPC via its coiled-coil domain.<ref>PMID:7559750</ref> <ref>PMID:9843582</ref> <ref>PMID:10801828</ref> <ref>PMID:10891509</ref> <ref>PMID:11739405</ref> <ref>PMID:11689687</ref> [[https://www.uniprot.org/uniprot/NUP98_MOUSE NUP98_MOUSE]] Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC (By similarity). [[https://www.uniprot.org/uniprot/NU159_YEAST NU159_YEAST]] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre-ribosome, and protein export.<ref>PMID:9736720</ref> <ref>PMID:9843582</ref> <ref>PMID:9891088</ref> <ref>PMID:10523319</ref> <ref>PMID:10801828</ref> <ref>PMID:10952996</ref> <ref>PMID:11387327</ref> <ref>PMID:11739405</ref> <ref>PMID:11689687</ref> <ref>PMID:12543930</ref> <ref>PMID:12604785</ref> <ref>PMID:15039779</ref> <ref>PMID:15574330</ref>
| + | [https://www.uniprot.org/uniprot/NUP82_YEAST NUP82_YEAST] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved as part of the NUP82-NUP159-NSP1 subcomplex in nuclear mRNA and pre-ribosome export by acting as a linker tethering nucleoporins that are directly involved in nuclear transport to the NPC via its coiled-coil domain.<ref>PMID:7559750</ref> <ref>PMID:9843582</ref> <ref>PMID:10801828</ref> <ref>PMID:10891509</ref> <ref>PMID:11739405</ref> <ref>PMID:11689687</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The cytoplasmic filament nucleoporins of the nuclear pore complex (NPC) are critically involved in nuclear export and remodeling of mRNA ribonucleoprotein particles and are associated with various human malignancies. Here, we report the crystal structure of the Nup98 C-terminal autoproteolytic domain, frequently missing from leukemogenic forms of the protein, in complex with the N-terminal domain of Nup82 and the C-terminal tail fragment of Nup159. The Nup82 beta propeller serves as a noncooperative binding platform for both binding partners. Interaction of Nup98 with Nup82 occurs through a reciprocal exchange of loop structures. Strikingly, the same Nup98 groove promiscuously interacts with Nup82 and Nup96 in a mutually excusive fashion. Simultaneous disruption of both Nup82 interactions in yeast causes severe defects in mRNA export, while the severing of a single interaction is tolerated. Thus, the cytoplasmic filament network of the NPC is robust, consistent with its essential function in nucleocytoplasmic transport.
| + | |
| - | | + | |
| - | Molecular Basis for the Anchoring of Proto-Oncoprotein Nup98 to the Cytoplasmic Face of the Nuclear Pore Complex.,Stuwe TT, von Borzyskowski LS, Davenport AM, Hoelz A J Mol Biol. 2012 Apr 2. PMID:22480613<ref>PMID:22480613</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3tkn" style="background-color:#fffaf0;"></div>
| + | |
| | | | |
| | ==See Also== | | ==See Also== |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Hoelz, A]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Stuwe, T T]] | + | [[Category: Hoelz A]] |
| - | [[Category: Oncoprotein]] | + | [[Category: Stuwe TT]] |
| - | [[Category: Protein complex]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| Structural highlights
Function
NUP82_YEAST Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved as part of the NUP82-NUP159-NSP1 subcomplex in nuclear mRNA and pre-ribosome export by acting as a linker tethering nucleoporins that are directly involved in nuclear transport to the NPC via its coiled-coil domain.[1] [2] [3] [4] [5] [6]
See Also
References
- ↑ Grandi P, Emig S, Weise C, Hucho F, Pohl T, Hurt EC. A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p. J Cell Biol. 1995 Sep;130(6):1263-73. PMID:7559750
- ↑ Belgareh N, Snay-Hodge C, Pasteau F, Dagher S, Cole CN, Doye V. Functional characterization of a Nup159p-containing nuclear pore subcomplex. Mol Biol Cell. 1998 Dec;9(12):3475-92. PMID:9843582
- ↑ Bailer SM, Balduf C, Katahira J, Podtelejnikov A, Rollenhagen C, Mann M, Pante N, Hurt E. Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex. J Biol Chem. 2000 Aug 4;275(31):23540-8. PMID:10801828 doi:http://dx.doi.org/10.1074/jbc.M001963200
- ↑ Ho AK, Shen TX, Ryan KJ, Kiseleva E, Levy MA, Allen TD, Wente SR. Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p. Mol Cell Biol. 2000 Aug;20(15):5736-48. PMID:10891509
- ↑ Gleizes PE, Noaillac-Depeyre J, Leger-Silvestre I, Teulieres F, Dauxois JY, Pommet D, Azum-Gelade MC, Gas N. Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex. J Cell Biol. 2001 Dec 10;155(6):923-36. Epub 2001 Dec 10. PMID:11739405 doi:http://dx.doi.org/10.1083/jcb.200108142
- ↑ Bailer SM, Balduf C, Hurt E. The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport. Mol Cell Biol. 2001 Dec;21(23):7944-55. PMID:11689687 doi:http://dx.doi.org/10.1128/MCB.21.23.7944-7955.2001
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