1uk5: Difference between revisions
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New page: left|200px<br /><applet load="1uk5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uk5" /> '''Solution structure of the Murine BAG domain ... |
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== | ==Solution structure of the Murine BAG domain of Bcl2-associated athanogene 3== | ||
<StructureSection load='1uk5' size='340' side='right'caption='[[1uk5]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1uk5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UK5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1uk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uk5 OCA], [https://pdbe.org/1uk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uk5 RCSB], [https://www.ebi.ac.uk/pdbsum/1uk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uk5 ProSAT], [https://www.topsan.org/Proteins/RSGI/1uk5 TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BAG3_MOUSE BAG3_MOUSE] Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uk/1uk5_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1uk5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ADP-ATP exchange by the molecular chaperone Hsp70 is enhanced by several cochaperones. BAG5 consists of five BAG domains and associates with the nucleotide-binding domain (NBD) of Hsp70. The overexpression of BAG5 in the cytosol reportedly disturbs Hsp70-mediated protein refolding and induces Parkinson's disease. In the present study, we found that the fifth BAG domain (BD5) of BAG5 is responsible for the interaction between Hsp70 and BAG5. We also determined the crystal structures of the BD5*NBD complex. BD5 binding caused two different types of NBD conformational changes, which both disrupted the nucleotide-binding groove. In fact, BD5 reduced the affinity of the NBD for ADP. Moreover, BD5, as well as the full-length BAG5, accelerated Hsp70-mediated refolding in an in vitro assay. Therefore, BAG5 can function as the nucleotide exchange factor of Hsp70 for the enhancement of protein refolding. | |||
The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange.,Arakawa A, Handa N, Ohsawa N, Shida M, Kigawa T, Hayashi F, Shirouzu M, Yokoyama S Structure. 2010 Mar 10;18(3):309-19. PMID:20223214<ref>PMID:20223214</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1uk5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Hatta R]] | |||
[[Category: Hatta | [[Category: Hayashi F]] | ||
[[Category: Hayashi | [[Category: Yokoyama S]] | ||
[[Category: Yoshida M]] | |||
[[Category: Yokoyama | |||
[[Category: Yoshida | |||
Latest revision as of 23:55, 27 December 2023
Solution structure of the Murine BAG domain of Bcl2-associated athanogene 3
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