5mkr: Difference between revisions

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-'''Unreleased structure'''
-The entry 5mkr is ON HOLD  until Paper Publication
+==HSP72-NBD bound to compound TCI 8 - Tyr15 in up-conformation==
+<StructureSection load='5mkr' size='340' side='right'caption='[[5mkr]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5mkr]] 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=5MKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MKR 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]] 1.87&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=TI8:3-[(2~{R},3~{S},4~{R},5~{R})-5-[6-AZANYL-8-[(4-CHLOROPHENYL)METHYLAMINO]PURIN-9-YL]-3,4-BIS(OXIDANYL)OXOLAN-2-YL]PROPYL+PROP-2-ENOATE'>TI8</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=5mkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mkr OCA], [https://pdbe.org/5mkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mkr RCSB], [https://www.ebi.ac.uk/pdbsum/5mkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mkr ProSAT]</span></td></tr>
+</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>
-Authors: Pettinger, J., Westwood, I.M., Cronin, N., Le Bihan, Y.-V., Van Montfort, R.L.M.
+==See Also==
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
-Description: HSP72-NBD bound to compound TCI 8 -Tyr15 in up-conformation
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Pettinger, J]]
+__TOC__
-[[Category: Van Montfort, R.L.M]]
+</StructureSection>
-[[Category: Westwood, I.M]]
+[[Category: Homo sapiens]]
-[[Category: Cronin, N]]
+[[Category: Large Structures]]
-[[Category: Le Bihan, Y.-V]]
+[[Category: Cronin N]]
+[[Category: Le Bihan Y-V]]
+[[Category: Pettinger J]]
+[[Category: Van Montfort RLM]]
+[[Category: Westwood IM]]