4god: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4god FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4god OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4god RCSB], [http://www.ebi.ac.uk/pdbsum/4god PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4god FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4god OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4god RCSB], [http://www.ebi.ac.uk/pdbsum/4god PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/SGTA_HUMAN SGTA_HUMAN]] Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity.<ref>PMID:18759457</ref> | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 10:25, 15 February 2015
Crystal structure of the SGTA homodimerization domainCrystal structure of the SGTA homodimerization domain
Structural highlights
Function[SGTA_HUMAN] Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity.[1] Publication Abstract from PubMedIn 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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