5xi9: Difference between revisions

<StructureSection load='5xi9' size='340' side='right'caption='[[5xi9]]' scene=''>

<table><tr><td colspan='2'>[[5xi9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XI9 FirstGlance]. <br>

</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=5xi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xi9 OCA], [https://pdbe.org/5xi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xi9 RCSB], [https://www.ebi.ac.uk/pdbsum/5xi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xi9 ProSAT]</span></td></tr>

[https://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: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Hoshikawa M]]

[[Category: Tate S]]

[[Category: Tochio N]]