5bpm

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'''Unreleased structure'''
 
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The entry 5bpm is ON HOLD until Paper Publication
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==Crystal structure of unhydrolyzed ATP bound human Hsp70 NBD double mutant E268Q+R272K.==
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<StructureSection load='5bpm' size='340' side='right'caption='[[5bpm]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5bpm]] 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=5BPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BPM FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.83&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5bpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bpm OCA], [https://pdbe.org/5bpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bpm RCSB], [https://www.ebi.ac.uk/pdbsum/5bpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bpm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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Authors: Narayanan, D., Engh, R.A.
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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Description: Crystal structure of unhydrolyzed ATP bound human Hsp70 NBD double mutant E268Q+R272K.
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Narayanan, D]]
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__TOC__
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[[Category: Engh, R.A]]
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Engh RA]]
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[[Category: Narayanan D]]

Current revision

Crystal structure of unhydrolyzed ATP bound human Hsp70 NBD double mutant E268Q+R272K.

PDB ID 5bpm

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