View source for 2lxb


==Solution structure of the Sgt2 homodimerization domain==
<StructureSection load='2lxb' size='340' side='right'caption='[[2lxb]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lxb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LXB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lxb OCA], [https://pdbe.org/2lxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lxb RCSB], [https://www.ebi.ac.uk/pdbsum/2lxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lxb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SGT2_YEAST SGT2_YEAST] Co-chaperone that binds to the molecular chaperone Hsp70 (SSA1 and SSA2). Regulates Hsp70 ATPase activity (By similarity). Required for recovery from heat shock.<ref>PMID:12482202</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In the cytoplasm, the correct delivery of membrane proteins is an essential and highly regulated process. The posttranslational targeting of the important tail-anchor membrane (TA) proteins has recently been under intense investigation. A specialized pathway, called the guided entry of TA proteins (GET) pathway in yeast and the transmembrane domain recognition complex (TRC) pathway in vertebrates, recognizes endoplasmic-reticulum-targeted TA proteins and delivers them through a complex series of handoffs. An early step is the formation of a complex between Sgt2/SGTA, a cochaperone with a presumed ubiquitin-like-binding domain (UBD), and Get5/UBL4A, a ubiquitin-like domain (UBL)-containing protein. We structurally characterize this UBD/UBL interaction for both yeast and human proteins. This characterization is supported by biophysical studies that demonstrate that complex formation is mediated by electrostatics, generating an interface that has high-affinity with rapid kinetics. In total, this work provides a refined model of the interplay of Sgt2 homologs in TA targeting.

Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface.,Chartron JW, Vandervelde DG, Clemons WM Jr Cell Rep. 2012 Nov 7. pii: S2211-1247(12)00346-4. doi:, 10.1016/j.celrep.2012.10.010. PMID:23142665<ref>PMID:23142665</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lxb" style="background-color:#fffaf0;"></div>

==See Also==
*[[Small glutamine-rich tetratricopeptide repeat containing protein alpha|Small glutamine-rich tetratricopeptide repeat containing protein alpha]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Chartron JW]]
[[Category: Clemons Jr WM]]
[[Category: Vandervelde DG]]