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< | ==Solution structure of the first Murine BAG domain of Bcl2-associated athanogene 5== | ||
<StructureSection load='1ugo' size='340' side='right'caption='[[1ugo]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ugo]] 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=1UGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UGO 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=1ugo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ugo OCA], [https://pdbe.org/1ugo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ugo RCSB], [https://www.ebi.ac.uk/pdbsum/1ugo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ugo ProSAT], [https://www.topsan.org/Proteins/RSGI/1ugo TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BAG5_MOUSE BAG5_MOUSE] May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity). | |||
== 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/ug/1ugo_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=1ugo 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 1ugo" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[BAG family proteins 3D structures|BAG family proteins 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Aoki | [[Category: Aoki M]] | ||
[[Category: Arakawa | [[Category: Arakawa T]] | ||
[[Category: Carninci | [[Category: Carninci P]] | ||
[[Category: Endoh | [[Category: Endoh H]] | ||
[[Category: Hayashi | [[Category: Hayashi F]] | ||
[[Category: Hayashizaki | [[Category: Hayashizaki Y]] | ||
[[Category: Hirota | [[Category: Hirota H]] | ||
[[Category: Inoue | [[Category: Inoue M]] | ||
[[Category: Kawai | [[Category: Kawai J]] | ||
[[Category: Kigawa | [[Category: Kigawa T]] | ||
[[Category: Matsuda | [[Category: Matsuda T]] | ||
[[Category: Osanai | [[Category: Osanai T]] | ||
[[Category: Seimiya K]] | |||
[[Category: Seimiya | [[Category: Seki E]] | ||
[[Category: Seki | [[Category: Shirouzu M]] | ||
[[Category: Shirouzu | [[Category: Tanaka A]] | ||
[[Category: Tanaka | [[Category: Terada T]] | ||
[[Category: Terada | [[Category: Yabuki T]] | ||
[[Category: Yabuki | [[Category: Yokoyama S]] | ||
[[Category: Yokoyama | [[Category: Yoshida M]] | ||
[[Category: Yoshida | |||
Latest revision as of 02:53, 28 December 2023
Solution structure of the first Murine BAG domain of Bcl2-associated athanogene 5Solution structure of the first Murine BAG domain of Bcl2-associated athanogene 5
Structural highlights
FunctionBAG5_MOUSE May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedADP-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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