View source for 5ywz


==AID-SUN tandem of SUN1==
<StructureSection load='5ywz' size='340' side='right'caption='[[5ywz]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ywz]] 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=5YWZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YWZ 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]] 2.2&#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=5ywz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ywz OCA], [https://pdbe.org/5ywz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ywz RCSB], [https://www.ebi.ac.uk/pdbsum/5ywz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ywz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SUN1_MOUSE SUN1_MOUSE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
LINC complexes span across the nuclear envelope and are assembled by SUN and KASH proteins. SUN1 and SUN2 are the two most abundant SUN proteins in mammals. In SUN2, the predicted coiled-coil domain preceding the SUN domain forms a three-helix bundle that constitutes an autoinhibitory domain (AID) to lock down the SUN domain. Here, we found that SUN1 also contains an AID preceding the SUN domain and solved the structure of the AID-SUN tandem of SUN1. SUN1 AID also adopts a three-helix bundle conformation that interacts with the SUN domain and keeps it in an autoinhibited state. Disruptions of the interaction interface in the AID-SUN tandem restored the SUN domain activity for binding to the KASH peptide. Structural comparison further demonstrated that the autoinhibited conformations of the AID-SUN tandems from SUN1 and SUN2 are similar and the intramolecular interdomain packing in SUN1 is slightly more compact than that in SUN2 due to minor variations of the residues in the interaction interface. Thus, AID is a conserved functional domain in SUN proteins and this work provides the structural evidence to support the conversation of the AID-mediated autoinhibition of SUN proteins.

Structural conservation of the autoinhibitory domain in SUN proteins.,Xu Y, Li W, Ke H, Feng W Biochem Biophys Res Commun. 2018 Feb 19;496(4):1337-1343. doi:, 10.1016/j.bbrc.2018.02.015. Epub 2018 Feb 3. PMID:29408528<ref>PMID:29408528</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ywz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Feng W]]
[[Category: Li W]]
[[Category: Xu Y]]