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==Structure of the Nup82-Nup159-Nup98 heterotrimer==
==Structure of the Nup82-Nup159-Nup98 heterotrimer==
<StructureSection load='3tkn' size='340' side='right' caption='[[3tkn]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<StructureSection load='3tkn' size='340' side='right'caption='[[3tkn]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3tkn]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://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 [http://oca.weizmann.ac.il/oca-docs/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><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HRB187, J1135, NUP82, YJL061W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), NUP158, NUP159, RAT7, YIL115C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), Nup98 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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]] 3.4&#8491;</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tkn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tkn RCSB], [http://www.ebi.ac.uk/pdbsum/3tkn PDBsum]</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>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[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>  
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>


==See Also==
==See Also==
*[[Nucleoporin|Nucleoporin]]
*[[Nucleoporin 3D structures|Nucleoporin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Hoelz, A.]]
[[Category: Hoelz A]]
[[Category: Stuwe, T T.]]
[[Category: Stuwe TT]]
[[Category: Oncoprotein]]
[[Category: Protein complex]]
[[Category: Protein transport]]

Latest revision as of 10:09, 1 March 2024

Structure of the Nup82-Nup159-Nup98 heterotrimer

3tkn, resolution 3.40Å

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