5e85: Difference between revisions

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-'''Unreleased structure'''
+==isolated SBD of BiP==
+<StructureSection load='5e85' size='340' side='right' caption='[[5e85]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5e85]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E85 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e84|5e84]], [[5e86|5e86]]</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=5e85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e85 OCA], [http://pdbe.org/5e85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e85 RCSB], [http://www.ebi.ac.uk/pdbsum/5e85 PDBsum]</span></td></tr>
+</table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/GRP78_HUMAN GRP78_HUMAN]] Note=Autoantigen in rheumatoid arthritis.<ref>PMID:11160188</ref>
+== Function ==
+[[http://www.uniprot.org/uniprot/GRP78_HUMAN GRP78_HUMAN]] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.<ref>PMID:2294010</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Binding immunoglobulin protein (BiP), an essential and ubiquitous Hsp70 chaperone in the ER, plays a key role in protein folding and quality control. BiP contains two functional domains: a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). NBD binds and hydrolyzes ATP; the substrates for SBD are extended polypeptides. ATP binding allosterically accelerates polypeptide binding and release. Although crucial to the chaperone activity, the molecular mechanisms of polypeptide binding and allosteric coupling of BiP are poorly understood. Here, we present crystal structures of an intact human BiP in the ATP-bound state, the first intact eukaryotic Hsp70 structure, and isolated BiP-SBD with a peptide substrate bound representing the ADP-bound state. These structures and our biochemical analysis demonstrate that BiP has a unique NBD-SBD interface that is highly conserved only in eukaryotic Hsp70s found in the cytosol and ER to fortify its ATP-bound state and promote the opening of its polypeptide-binding pocket.
-The entry 5e85 is ON HOLD  until Paper Publication
+Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP.,Yang J, Nune M, Zong Y, Zhou L, Liu Q Structure. 2015 Dec 1;23(12):2191-203. doi: 10.1016/j.str.2015.10.012. Epub 2015 , Nov 19. PMID:26655470<ref>PMID:26655470</ref>
-Authors: Liu, Q., Yang, J., Nune, M., Zong, Y., Zhou, L.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: isolated SBD of BiP
+<div class="pdbe-citations 5e85" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
-[[Category: Zong, Y]]
+<references/>
-[[Category: Yang, J]]
+__TOC__
+</StructureSection>
 [[Category: Liu, Q]]
 [[Category: Nune, M]]
+[[Category: Yang, J]]
 [[Category: Zhou, L]]
+[[Category: Zong, Y]]
+[[Category: Allosteric coupling]]
+[[Category: Bip]]
+[[Category: Chaperone]]
+[[Category: Endoplasmic reticulum]]
+[[Category: Hsp70]]
+[[Category: Molecular chaperone]]
+[[Category: Protein folding]]