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4i0o

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'''Unreleased structure'''
 
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The entry 4i0o is ON HOLD until Paper Publication
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==Nucleoporin ELYS (aa1-494), Mus musculus==
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<StructureSection load='4i0o' size='340' side='right'caption='[[4i0o]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4i0o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I0O FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4i0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i0o OCA], [https://pdbe.org/4i0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i0o RCSB], [https://www.ebi.ac.uk/pdbsum/4i0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i0o ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ELYS_MOUSE ELYS_MOUSE] Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex of the NPC. Also required for the localization of the Nup107-160 subcomplex of the NPC to the kinetochore during mitosis and for the completion of cytokinesis (By similarity). Has also been proposed to function as a transcription factor which may play a specific role in hematopoietic tissues (PubMed:11952839).<ref>PMID:11952839</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In metazoa, the nuclear envelope (NE), together with the embedded nuclear pore complexes (NPCs), breaks down and reassembles during cell division. It is suggested that ELYS, a nucleoporin, binds to chromatin in an initial step of postmitotic NPC assembly and subsequently recruits the essential Y-subcomplex, the major scaffolding unit of the NPC. Here, we show that ELYS contains three domains: an N-terminal beta-propeller domain, a central alpha-helical domain, and a C-terminal disordered region. While the disordered region is responsible for the interactions with chromatin, the two preceding domains synergistically mediate tethering to the NPC. We present the crystal structure of the seven-bladed beta-propeller domain at 1.9 A resolution. Analysis of the beta-propeller surface reveals the regions that are required for NPC anchorage. We discuss the possible roles of ELYS in the context of the NPC scaffold architecture.
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Authors: Bilokapic, S.
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Structural and Functional Studies of the 252 kDa Nucleoporin ELYS Reveal Distinct Roles for Its Three Tethered Domains.,Bilokapic S, Schwartz TU Structure. 2013 Apr 2;21(4):572-80. doi: 10.1016/j.str.2013.02.006. Epub 2013 Mar, 14. PMID:23499022<ref>PMID:23499022</ref>
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Description: Structure of the WD repeat-containing protein
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4i0o" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Bilokapic S]]
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[[Category: Schwartz TU]]

Current revision

Nucleoporin ELYS (aa1-494), Mus musculus

PDB ID 4i0o

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