5aqw
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues== | |
| - | + | <StructureSection load='5aqw' size='340' side='right' caption='[[5aqw]], [[Resolution|resolution]] 1.53Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5aqw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AQW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AQW FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5P7:(1S,2R,3R,5R)-3-(HYDROXYMETHYL)-5-(QUINAZOLIN-4-YLAMINO)CYCLOPENTANE-1,2-DIOL'>5P7</scene>, <scene name='pdbligand=DTV:(2S,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTV</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5aqf|5aqf]], [[5aqg|5aqg]], [[5aqh|5aqh]], [[5aqi|5aqi]], [[5aqj|5aqj]], [[5aqk|5aqk]], [[5aql|5aql]], [[5aqm|5aqm]], [[5aqn|5aqn]], [[5aqo|5aqo]], [[5aqp|5aqp]], [[5aqq|5aqq]], [[5aqr|5aqr]], [[5aqs|5aqs]], [[5aqt|5aqt]], [[5aqu|5aqu]], [[5aqv|5aqv]], [[5aqx|5aqx]], [[5aqy|5aqy]], [[5aqz|5aqz]], [[5ar0|5ar0]]</td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mitochondrial_protein-transporting_ATPase Mitochondrial protein-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.51 3.6.3.51] </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=5aqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aqw OCA], [http://pdbe.org/5aqw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aqw RCSB], [http://www.ebi.ac.uk/pdbsum/5aqw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aqw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Mitochondrial protein-transporting ATPase]] | ||
[[Category: Burke, R]] | [[Category: Burke, R]] | ||
| - | [[Category: | + | [[Category: Cheeseman, M D]] |
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[[Category: Collins, I]] | [[Category: Collins, I]] | ||
| - | [[Category: | + | [[Category: Dobson, S E]] |
| + | [[Category: Jeganathan, F]] | ||
| + | [[Category: Jones, A M]] | ||
[[Category: Jones, K]] | [[Category: Jones, K]] | ||
| - | [[Category: | + | [[Category: Kadi, N]] |
| - | [[Category: | + | [[Category: Lee, D]] |
| - | [[Category: | + | [[Category: Liu, M]] |
| - | [[Category: | + | [[Category: Matthews, T P]] |
| + | [[Category: McAndrew, C]] | ||
| + | [[Category: Montfort, R L.M van]] | ||
| + | [[Category: Osborne, J D]] | ||
[[Category: Richards, M]] | [[Category: Richards, M]] | ||
| - | [[Category: | + | [[Category: Rowlands, M G]] |
| - | [[Category: | + | [[Category: Westwood, I M]] |
| - | [[Category: | + | [[Category: Workman, P]] |
| - | [[Category: | + | [[Category: Yahya, N]] |
| + | [[Category: Atpase]] | ||
| + | [[Category: Bag1]] | ||
| + | [[Category: Chaperone]] | ||
| + | [[Category: Fragment]] | ||
| + | [[Category: Heat shock protein]] | ||
| + | [[Category: Hsc70]] | ||
| + | [[Category: Hsp70]] | ||
| + | [[Category: Hsp72]] | ||
Revision as of 21:21, 5 October 2016
Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues
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Categories: Mitochondrial protein-transporting ATPase | Burke, R | Cheeseman, M D | Collins, I | Dobson, S E | Jeganathan, F | Jones, A M | Jones, K | Kadi, N | Lee, D | Liu, M | Matthews, T P | McAndrew, C | Montfort, R L.M van | Osborne, J D | Richards, M | Rowlands, M G | Westwood, I M | Workman, P | Yahya, N | Atpase | Bag1 | Chaperone | Fragment | Heat shock protein | Hsc70 | Hsp70 | Hsp72
