7t5p: Difference between revisions

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'''Unreleased structure'''


The entry 7t5p is ON HOLD  until Paper Publication
==Cryo-EM structure of human SIMC1-SLF2 complex==
<StructureSection load='7t5p' size='340' side='right'caption='[[7t5p]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7t5p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T5P FirstGlance]. <br>
</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=7t5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t5p OCA], [https://pdbe.org/7t5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t5p RCSB], [https://www.ebi.ac.uk/pdbsum/7t5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t5p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SIMC1_HUMAN SIMC1_HUMAN] Inhibits the protease activity of CAPN3.<ref>PMID:23707407</ref>  Inhibits the protease activity of CAPN3.<ref>PMID:23707407</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The human SMC5/6 complex is a conserved guardian of genome stability and an emerging component of antiviral responses. These disparate functions likely require distinct mechanisms of SMC5/6 regulation. In yeast, Smc5/6 is regulated by its Nse5/6 subunits, but such regulatory subunits for human SMC5/6 are poorly defined. Here, we identify a novel SMC5/6 subunit called SIMC1 that contains SUMO interacting motifs (SIMs) and an Nse5-like domain. We isolated SIMC1 from the proteomic environment of SMC5/6 within polyomavirus large T antigen (LT)-induced subnuclear compartments. SIMC1 uses its SIMs and Nse5-like domain to localize SMC5/6 to polyomavirus replication centers (PyVRCs) at SUMO-rich PML nuclear bodies. SIMC1's Nse5-like domain binds to the putative Nse6 orthologue SLF2 to form an anti-parallel helical dimer resembling the yeast Nse5/6 structure. SIMC1-SLF2 structure-based mutagenesis defines a conserved surface region containing the N-terminus of SIMC1's helical domain that regulates SMC5/6 localization to PyVRCs. Furthermore, SLF1, which recruits SMC5/6 to DNA lesions via its BRCT and ARD motifs, binds SLF2 analogously to SIMC1 and forms a separate Nse5/6-like complex. Thus, two Nse5/6-like complexes with distinct recruitment domains control human SMC5/6 localization.


Authors:  
The Nse5/6-like SIMC1-SLF2 complex localizes SMC5/6 to viral replication centers.,Oravcova M, Nie M, Zilio N, Maeda S, Jami-Alahmadi Y, Lazzerini-Denchi E, Wohlschlegel JA, Ulrich HD, Otomo T, Boddy MN Elife. 2022 Nov 14;11:e79676. doi: 10.7554/eLife.79676. PMID:36373674<ref>PMID:36373674</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 7t5p" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Boddy MN]]
[[Category: Maeda S]]
[[Category: Oravcova M]]
[[Category: Otomo T]]
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