2d9d: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5== | ==Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5== | ||
<StructureSection load='2d9d' size='340' side='right' caption='[[2d9d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2d9d' size='340' side='right'caption='[[2d9d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2d9d]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2d9d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D9D FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAG5 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAG5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2d9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d9d OCA], [https://pdbe.org/2d9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d9d RCSB], [https://www.ebi.ac.uk/pdbsum/2d9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d9d ProSAT], [https://www.topsan.org/Proteins/RSGI/2d9d TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/BAG5_HUMAN BAG5_HUMAN]] Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity). May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding.<ref>PMID:20223214</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[BAG | *[[BAG family proteins 3D structures|BAG family proteins 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 26: | Line 26: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Hatta, R]] | [[Category: Hatta, R]] | ||
[[Category: Hayashi, F]] | [[Category: Hayashi, F]] | ||
Revision as of 14:56, 3 February 2021
Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5
Structural highlights
Function[BAG5_HUMAN] Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity). May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding.[1] 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||