3atv
From Proteopedia
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| - | [[Image:3atv.png|left|200px]] | ||
| - | + | ==Crystal structure of human Hsp70 NBD in the ADP-bound and Mg ion-free state== | |
| - | + | <StructureSection load='3atv' size='340' side='right'caption='[[3atv]], [[Resolution|resolution]] 1.58Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3atv]] 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=3ATV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ATV FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58Å</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=3atv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3atv OCA], [https://pdbe.org/3atv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3atv RCSB], [https://www.ebi.ac.uk/pdbsum/3atv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3atv ProSAT]</span></td></tr> |
| - | [[3atv]] is a 1 chain structure with sequence from [ | + | </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> | ||
==See Also== | ==See Also== | ||
| - | *[[Heat Shock | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Arakawa | + | [[Category: Large Structures]] |
| - | [[Category: Handa | + | [[Category: Arakawa A]] |
| - | [[Category: Shirouzu | + | [[Category: Handa N]] |
| - | [[Category: Yokoyama | + | [[Category: Shirouzu M]] |
| - | + | [[Category: Yokoyama S]] | |
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Current revision
Crystal structure of human Hsp70 NBD in the ADP-bound and Mg ion-free state
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