5bpl

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'''Unreleased structure'''
 
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The entry 5bpl is ON HOLD until Paper Publication
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==Crystal structure of ADP and Pi bound human Hsp70 NBD mutant R272K.==
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<StructureSection load='5bpl' size='340' side='right' caption='[[5bpl]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
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Authors: Narayanan, D., Engh, R.A.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5bpl]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BPL FirstGlance]. <br>
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Description: Crystal structure of ADP and Pi bound human Hsp70 NBD mutant R272K.
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</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bn8|5bn8]], [[5bn9|5bn9]], [[5bpm|5bpm]], [[5bpn|5bpn]]</td></tr>
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<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=5bpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bpl OCA], [http://pdbe.org/5bpl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bpl RCSB], [http://www.ebi.ac.uk/pdbsum/5bpl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bpl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Engh, R A]]
[[Category: Narayanan, D]]
[[Category: Narayanan, D]]
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[[Category: Engh, R.A]]
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[[Category: Atp hydrolysis activity]]
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[[Category: Hydrolase]]

Revision as of 15:27, 14 September 2016

Crystal structure of ADP and Pi bound human Hsp70 NBD mutant R272K.

5bpl, resolution 1.93Å

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