View source for 3hxr


==Nucleoporin Nup120 from S.cerevisiae (aa 1-757)==
<StructureSection load='3hxr' size='340' side='right'caption='[[3hxr]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3hxr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HXR FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NUP120, RAT2, YKL057C, YKL314, YKL313 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3hxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hxr OCA], [https://pdbe.org/3hxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hxr RCSB], [https://www.ebi.ac.uk/pdbsum/3hxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hxr ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/NU120_YEAST NU120_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. NUP120 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization.<ref>PMID:8557737</ref> <ref>PMID:8565072</ref> <ref>PMID:11071906</ref> <ref>PMID:11823431</ref> <ref>PMID:12730220</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hx/3hxr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hxr ConSurf].
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== Publication Abstract from PubMed ==
Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous protein assemblies residing in circular openings in the nuclear envelope. The NPC is modular, with transient and stable components. The stable core is essentially built from two multiprotein complexes, the Y-shaped heptameric Nup84 complex and the Nic96 complex, arranged around an eightfold axis. We present the crystal structure of Nup120(1-757), one of the two short arms of the Y-shaped Nup84 complex. The protein adopts a compact oval shape built around a novel bipartite alpha-helical domain intimately integrated with a beta-propeller domain. The domain arrangement is substantially different from the Nup85*Seh1 complex, which forms the other short arm of the Y. With the data presented here, we establish that all three branches of the Y-shaped Nup84 complex are tightly connected by helical interactions and that the beta-propellers likely form interaction site(s) to neighboring complexes.

The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture.,Leksa NC, Brohawn SG, Schwartz TU Structure. 2009 Aug 12;17(8):1082-91. Epub 2009 Jul 2. PMID:19576787<ref>PMID:19576787</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3hxr" style="background-color:#fffaf0;"></div>

==See Also==
*[[Nucleoporin 3D structures|Nucleoporin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Brohawn, S G]]
[[Category: Leksa, N C]]
[[Category: Schwartz, T U]]
[[Category: Coiled coil]]
[[Category: Membrane]]
[[Category: Mrna transport]]
[[Category: Nuclear pore complex]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: Protein transport]]
[[Category: Structural protein]]
[[Category: Translocation]]
[[Category: Transport]]