View source for 6wg4


==Crystal structure of human SMC1-SMC3 hinge domain heterodimer in south-open conformation==
<StructureSection load='6wg4' size='340' side='right'caption='[[6wg4]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6wg4]] 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=6WG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WG4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.31&#8491;</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=6wg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wg4 OCA], [https://pdbe.org/6wg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wg4 RCSB], [https://www.ebi.ac.uk/pdbsum/6wg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wg4 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/SMC1A_HUMAN SMC1A_HUMAN] Cornelia de Lange syndrome;Wiedemann-Steiner syndrome. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/SMC1A_HUMAN SMC1A_HUMAN] Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.<ref>PMID:11877377</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
As a ring-shaped ATPase machine, cohesin organizes the eukaryotic genome by extruding DNA loops and mediates sister-chromatid cohesion by topologically entrapping DNA. How cohesin executes these fundamental DNA transactions is not understood. Using cryo-electron microscopy, we determine the structure of human cohesin bound to its loader NIPBL and DNA at medium resolution. Cohesin and NIPBL interact extensively and together form a central tunnel to entrap a 72-base pair DNA. NIPBL and DNA promote the engagement of cohesin's ATPase head domains and ATP binding. The hinge domains of cohesin adopt an "open washer" conformation and dock onto the STAG1 subunit. Our structure explains the synergistic activation of cohesin by NIPBL and DNA, and provides insight into DNA entrapment by cohesin.

Cryo-EM structure of the human cohesin-NIPBL-DNA complex.,Shi Z, Gao H, Bai XC, Yu H Science. 2020 May 14. pii: science.abb0981. doi: 10.1126/science.abb0981. PMID:32409525<ref>PMID:32409525</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6wg4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Shi ZB]]
[[Category: Yu H]]