6k39: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6k39 is ~~ON HOLD until Paper Publication~~

==Structural analysis of AIMP2-DX2 and HSP70 interaction==

~~Authors~~: ~~Cho~~, H.Y., ~~Son~~, S.Y., ~~Jeon~~, Y.H.

== Structural highlights ==

<table><tr><td colspan='2'>[[6k39]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K39 FirstGlance]. <br>

~~Description~~: ~~Structural analysis~~ of ~~AIMP2~~-~~DX2~~ and ~~HSP70 interaction~~

</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=6k39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k39 OCA], [http://pdbe.org/6k39 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k39 RCSB], [http://www.ebi.ac.uk/pdbsum/6k39 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k39 ProSAT]</span></td></tr>

[[Category: ~~Unreleased~~ Structures]]

</table>

[[Category: ~~Jeon~~, Y.H]]

== Function ==

[[Category: ~~Cho~~, H.Y]]

[[http://www.uniprot.org/uniprot/HS71A_HUMAN HS71A_HUMAN]] In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).<ref>PMID:16537599</ref> <ref>PMID:22528486</ref> <ref>PMID:23973223</ref>

[[Category: Son, S.Y]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Cho, H Y]]

[[Category: Jeon, Y H]]

[[Category: Son, S Y]]

[[Category: Aimp2-dx2]]

[[Category: Chaperone]]

[[Category: Hsp70]]

[[Category: Substrate binding domain]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6k39 is ON HOLD  until Paper Publication
+==Structural analysis of AIMP2-DX2 and HSP70 interaction==
+<StructureSection load='6k39' size='340' side='right'caption='[[6k39]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
-Authors: Cho, H.Y., Son, S.Y., Jeon, Y.H.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6k39]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K39 FirstGlance]. <br>
-Description: Structural analysis of AIMP2-DX2 and HSP70 interaction
+</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=6k39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k39 OCA], [http://pdbe.org/6k39 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k39 RCSB], [http://www.ebi.ac.uk/pdbsum/6k39 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k39 ProSAT]</span></td></tr>
-[[Category: Unreleased Structures]]
+</table>
-[[Category: Jeon, Y.H]]
+== Function ==
-[[Category: Cho, H.Y]]
+[[http://www.uniprot.org/uniprot/HS71A_HUMAN HS71A_HUMAN]] In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).<ref>PMID:16537599</ref> <ref>PMID:22528486</ref> <ref>PMID:23973223</ref>
-[[Category: Son, S.Y]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Cho, H Y]]
+[[Category: Jeon, Y H]]
+[[Category: Son, S Y]]
+[[Category: Aimp2-dx2]]
+[[Category: Chaperone]]
+[[Category: Hsp70]]
+[[Category: Substrate binding domain]]