3jxu: Difference between revisions

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<StructureSection load='3jxu' size='340' side='right'caption='[[3jxu]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
<StructureSection load='3jxu' size='340' side='right'caption='[[3jxu]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3jxu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JXU FirstGlance]. <br>
<table><tr><td colspan='2'>[[3jxu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JXU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JXU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i33|3i33]], [[3gdq|3gdq]], [[3iuc|3iuc]], [[3fe1|3fe1]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=3jxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jxu OCA], [http://pdbe.org/3jxu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jxu RCSB], [http://www.ebi.ac.uk/pdbsum/3jxu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jxu ProSAT]</span></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=3jxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jxu OCA], [https://pdbe.org/3jxu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jxu RCSB], [https://www.ebi.ac.uk/pdbsum/3jxu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jxu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Berg, S Van Den]]
[[Category: Berglund H]]
[[Category: Berglund, H]]
[[Category: Bountra C]]
[[Category: Bountra, C]]
[[Category: Collins R]]
[[Category: Collins, R]]
[[Category: Edwards AM]]
[[Category: Edwards, A M]]
[[Category: Flodin S]]
[[Category: Flodin, S]]
[[Category: Flores A]]
[[Category: Flores, A]]
[[Category: Graslund S]]
[[Category: Graslund, S]]
[[Category: Hammarstrom M]]
[[Category: Hammarstrom, M]]
[[Category: Johansson A]]
[[Category: Johansson, A]]
[[Category: Johansson I]]
[[Category: Johansson, I]]
[[Category: Kallas A]]
[[Category: Kallas, A]]
[[Category: Karlberg T]]
[[Category: Karlberg, T]]
[[Category: Kotenyova T]]
[[Category: Kotenyova, T]]
[[Category: Kotzsch A]]
[[Category: Kotzsch, A]]
[[Category: Kraulis P]]
[[Category: Kraulis, P]]
[[Category: Markova N]]
[[Category: Markova, N]]
[[Category: Moche M]]
[[Category: Moche, M]]
[[Category: Nielsen TK]]
[[Category: Nielsen, T K]]
[[Category: Nordlund P]]
[[Category: Nordlund, P]]
[[Category: Nyman T]]
[[Category: Nyman, T]]
[[Category: Persson C]]
[[Category: Persson, C]]
[[Category: Roos AK]]
[[Category: Roos, A K]]
[[Category: Schuler H]]
[[Category: Structural genomic]]
[[Category: Schutz P]]
[[Category: Schuler, H]]
[[Category: Siponen MI]]
[[Category: Schutz, P]]
[[Category: Svensson L]]
[[Category: Siponen, M I]]
[[Category: Thorsell AG]]
[[Category: Svensson, L]]
[[Category: Tresaugues L]]
[[Category: Thorsell, A G]]
[[Category: Van Den Berg S]]
[[Category: Tresaugues, L]]
[[Category: Wahlberg E]]
[[Category: Wahlberg, E]]
[[Category: Weigelt J]]
[[Category: Weigelt, J]]
[[Category: Welin M]]
[[Category: Welin, M]]
[[Category: Wisniewska MM]]
[[Category: Wisniewska, M M]]
[[Category: Atp-binding]]
[[Category: Chaperone]]
[[Category: Helix]]
[[Category: Nucleotide-binding]]
[[Category: Phosphoprotein]]
[[Category: Polymorphism]]
[[Category: Sgc]]
[[Category: Stress response]]
Retrieved from "https://proteopedia.org/3jxu"